Подбор новых молекулярных мишеней для оптимизации вакцинопрофилактики и терапии чумы
- Авторы: Красильникова Е.А.1, Трунякова А.С.1, Вагайская А.С.1, Светоч Т.Э.1, Шайхутдинова Р.З.1, Дентовская С.В.1
-
Учреждения:
- Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
- Выпуск: Том 11, № 2 (2021)
- Страницы: 265-282
- Раздел: ОБЗОРЫ
- Дата подачи: 19.07.2019
- Дата принятия к публикации: 26.11.2019
- Дата публикации: 05.06.2020
- URL: https://iimmun.ru/iimm/article/view/1254
- DOI: https://doi.org/10.15789/2220-7619-SNM-1254
- ID: 1254
Цитировать
Полный текст
Аннотация
Возбудитель чумы, Yersinia pestis, — особо опасный бактериальный патоген и потенциальный агент биотерроризма. Преобладающими клиническими формами инфекции являются бубонная и легочная чума, отличающиеся путем инфицирования. При отсутствии лечения смертность при бубонной форме чумы составляет 40—60%, в то время как легочная чума без лечения летальна всегда. Развитие инфекционного процесса в организме восприимчивого хозяина обеспечивается наличием у чумного микроба комплекса факторов патогенности различной функциональной направленности, экспрессирующихся в зависимости от стадии инфекционного процесса. Нокаутные мутации генов, кодирующих эти факторы, могут не влиять на вирулентность микроба или приводить к его аттенуации. Поиск новых факторов патогенности Y. pestis и разработка на их основе высокоэффективных субъединичных и живых чумных вакцин, индуцирующих развитие выраженных клеточных и гуморальных иммунных реакций, и/или оценка потенциального использования этих факторов в качестве молекулярных мишеней для химиотерапии чумы остаются по-прежнему актуальными, так как обе лицензированные на настоящий день чумные вакцины не соответствуют требованиям ВОЗ, а на Мадагаскаре выделены штаммы чумного микроба, устойчивые ко всем лекарственным препаратам, рекомендованным для антибактериальной терапии чумы. В настоящей статье обобщены сведения относительно вклада известных и вновь открытых факторов патогенности в вирулентность штаммов Y. pestis и протективную активность в отношении чумы. Описано также влияние утраты генов регуляторных белков и мутаций в генах различных транспортных систем Y. pestis на аттенуацию вирулентных штаммов. Проведена оценка перспективности включения охарактеризованных антигенов в состав прототипов субъединичных вакцин и тех или иных полученных мутантов в состав прототипов живых аттенуированных вакцин. Использование антибиотиков постулируется комитетом экспертов Всемирной организации здравоохранения по чуме как «золотой стандарт» лечения чумы. Однако появление устойчивых к антибиотикам штаммов Y. pestis привело к необходимости поиска альтернативных способов терапии. В обзоре обобщены предварительные результаты попыток лечения чумы ингибиторами фактора патогенности. Препараты, нацеленные на ключевые факторы патогенности, предоставляют новые перспективные возможности в борьбе с устойчивыми к антибиотикам бактериями.
Ключевые слова
Об авторах
Е. А. Красильникова
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Email: krasilnikowa.katya111@yandex.ru
Младший научный сотрудник лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
РоссияА. С. Трунякова
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Email: Sasha_trunyakova@mail.ru
ORCID iD: 0000-0001-9223-2105
Стажер-исследователь лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
SPIN-код: 7290-1420
РоссияА. С. Вагайская
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Email: vagaiskaya.anastasiya@gmail.com
ORCID iD: 0000-0001-7280-3660
Младший научный сотрудник лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
РоссияТ. Э. Светоч
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Email: tanyasvetoch@yandex.ru
Научный сотрудник лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
РоссияР. З. Шайхутдинова
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Email: shaikhutdinova@yandex.ru
ORCID iD: 0000-0002-6985-6822
Старший научный сотрудник лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
РоссияС. В. Дентовская
Государственный научный центр прикладной микробиологии и биотехнологии Роспотребнадзора
Автор, ответственный за переписку.
Email: dentovskaya@yandex.ru
ORCID iD: 0000-0002-1996-8949
Дентовская Светлана Владимировна - доктор медицинских наук, главный научный сотрудник лаборатории микробиологии чумы отдела особо опасных инфекций.
142279, Московская область, Серпуховский р-н, п. Оболенск.
Тел.: 8 (4967) 36-01-17
SPIN-код: 4861-5248
РоссияСписок литературы
- Анисимов А.П. Факторы Yersinia pestis, обеспечивающие циркуляцию и сохранение возбудителя чумы в экосистемах природных очагов. Сообщение 2 // Молекул. генетика, микробиология и вирусология, 2002. № 3. С. 3-23.
- Дальвадянц С.М., Дятлов И.А., Еремин С.А., Щуковская Т.Н., Саяпина Л.В., Сергеева Г.М., Кутырев В.В. Исследования по иммунизации против чумы. Сообщение 4. Опыт ревакцинации волонтеров "химической" и живой чумной вакцинами // Проблемы особо опасных инфекций, 2006. № 91. C. 57-61.
- Наумов А.В., Ледванов М.Ю., Дроздов И.Г. Иммунология чумы. Саратов, 1992. 172 с.
- Achouak W., Heulin T., Pagès J.M. Multiple facets of bacterial porins. Protein Sci., 2001, vol. 199, no. 1, pp. 1-7.
- Achtman M., Zurth K., Morelli G., Torrea G., Guiyoule A., Carniel E. Yersinia pestis, the cause of plague, is a recently emerged clone of Yersinia pseudotuberculosis. Proc. Natl. Acad. Sci. USA, 1999, vol. 96, pp. 14043-14048.
- Ackermann N., Tiller M., Anding G., Roggenkamp A., Heesemann J. Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica. Journal of bacteriology, 2008, vol. 190, pp. 5031-5043.
- Aliprantis A.O., Yang R.B., Mark M.R., Suggett S., Devaux B., Radolf J.D., Klimpel G.R., Godowski P., Zychlinsky A. Cell activation and apoptosis by bacterial lipoproteins through toll-like receptor-2. Science, 1999, vol. 285, pp. 736-739.
- Anderson E.S., Paulley J.T., Gaines J.M., Valderas M.W., Martin D.W., Menscher E., Brown T.D., Burns C.S., Roop R.M. The manganese transporter MntH is a critical virulence determinant for Brucella abortus 2308 in experimentally infected mice. Infect. Immun., 2009, vol. 77, pp. 3466–3474. doi: 10.1128/IAI.00444-09
- Andersson J.A., Sha J., Erova T.E., Fitts E.C., Ponnusamy D., Kozlova E.V., Kirtley M.L., Chopra A.K. Identification of New Virulence Factors and Vaccine Candidates for Yersinia pestis. Front Cell Infect. Microbiol., 2017, vol. 7, pp. 448. doi: 10.3389/fcimb.2017.00448
- Andrews G.P., Strachan S.T., Benner G.E. Protective efficacy of recombinant Yersinia outer proteins against bubonic plague caused by encapsulated and non-encapsulated Yersinia pestis. Infect. Immun., 1999, vol. 67, pp. 1533-1537.
- Anisimov A.P. Factors providing the blocking activity of Yersinia pestis. Mol. Gen. Mikrobiol. Virusol., 1999, vol. 4, pp. 11-15.
- Anisimov A.P., Amoako K.K. Treatment of plague: promising alternatives to antibiotics. J. Med. Microbiol., 2006, vol. 55, pp. 1461-1475.
- Anisimov A.P., Dentovskaya S.V., Panfertsev E.A., Svetoch T.E., Kopylov P.Kh., Segelke B.W., Zemla A., Telepnev M.V., Motin V.L. Amino acid and structural variability of Yersinia pestis LcrV protein. Infect. Genet. Evol., 2010, vol. 10, pp. 137-145.
- Anisimov A.P., Lindler L.E., Pier G.B. Intraspecific diversity of Yersinia pestis. Clin. Microbiol. Rev., 2004, vol. 17, no. 2, pp. 434-464.
- Arirachakaran P., Benjavongkulchai E., Luengpailin S., Ajdić D., Banas J.A. Manganese affects Streptococcus mutans virulence gene expression. Caries Res., 2007, vol. 41(6), pp. 503-11.
- Auerbuch V., Loureiro J.J., Gertler F.B., Theriot J.A., Portnoy D.A. Ena/VASP proteins contribute to Listeria monocytogenes pathogenesis by controlling temporal and spatial persistence of bacterial actin-based motility. Mol. Microbiol., 2003, vol. 49, no. 5, pp. 1361-1375.
- Bartra S.S., Gong X., Lorica C.D., Jain C., Nair M.K., Schifferli D., Qian L., Li Z., Plano G.V, Schesser. K. The outer membrane protein A (OmpA) of Yersinia pestis promotes intracellular survival and virulence in mice. Microb. Pathog., 2012, vol. 52, no. 1, pp. 41-46.
- Bartra S.S., Styer K.L., O'Bryant D.M., Nilles M.L., Hinnebusch B.J., Aballay A., Plano G.V. Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein. Infect. Immun., 2008, vol. 76, pp. 612-622.
- Bear J.E., Gertler F.B. Ena/VASP: towards resolving a pointed controversy at the barbed end. J. Cell Sci. 2009, vol. 122, pp. 1947-1953.
- Bearden S. W., Staggs T. M., Perry R. D. An ABC transporter system of Yersinia pestisallows utilization of chelated iron by Escherichia coli SAB11. J. Bacteriol., 1998, vol. 180, pp. 1135–1147.
- Bearden S.W., Perry R.D. The Yfe system of Yersinia pestis transports iron and manganese and is required for full virulence of plague. Mol. Microbiol., 1999, vol. 32, pp. 403–414. doi: 10.1046/j.1365-2958.1999.01360.x
- Behrens S., Kneip S. The role of SurA factor in outer membrane protein transport and virulence. Int. J. Med. Microbiol., 2010, vol. 300, pp. 421-428.
- Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J., 2001, vol. 15, pp. 285-294.
- Berry A. M., Paton J. C. Sequence heterogeneity of PsaA, a 37-kilodalton putative adhesin essential for virulence of Streptococcus pneumonia. Infect. Immun., 1996, vol 64, pp. 5255–5262.
- Bierne H., Miki H., Innocenti M., Scita G., Gertler F.B., Takenawa T. WASP-related proteins, Abi1 and Ena/VASP are required for Listeria invasion induced by the Met receptor. J Cell Sci., 2005, vol. 118, pp. 1537-1547.
- Blaylock B., Berube B.J., Schneewind O. YopR impacts type III needle polymerization in Yersinia species. Mol. Microbiol., 2010, vol. 75, pp. 221–229.
- Bobrov A.G., Kirillina O., Fetherston J.D., Miller M.C., Burlison J.A., Perry R.D. The Yersinia pestis siderophore, yersiniabactin, and the ZnuABC system both contribute to Zinc acquisition and the development of lethal septicemic plague in mice. Mol. Microbiol., 2014, vol. 93, pp. 759–775.
- Bobrov A.G., Kirillina O., Fosso M.Y., Fetherston J.D., Miller M.C., van Cleave T.T. Zinc transporters YbtX and ZnuABC are required for the virulence of Yersinia pestis in bubonic and pneumonic plague in mice. Metallomics, 2017, vol. 21, pp. 757–772. doi: 10.1039/c7mt00126f
- Bobrov A.G., Kirillina O., Ryjenkov D.A., Waters C.M., Price P.A., Fetherston J.D. Systematic analysis of cyclic di-GMP signalling enzymes and their role in biofilm formation and virulence in Yersinia pestis. Mol. Microbiol., 2011, vol. 79, no. 2, pp. 533-551.
- Boyer E., Bergevin I., Malo D., Gros P., Cellier M. F. M. Acquisition of Mn(II) in addition to Fe(II) is required for full virulence of Salmonella enterica serovar Typhimurium. Infect. Immun., 2002, vol. 70, pp. 6032–6042. doi: 10.1128/IAI.70.11.6032-6042.2002
- Brannon J.R., Burk D.L., Leclerc J.M., Thomassin J.L., Portt A., Berghuis A.M., Gruenheid S., Le Moual H. Inhibition of outer membrane proteases of the omptin family by aprotinin. Infect. Immun., 2015, vol. 83, no. 6, pp. 2300-11. doi: 10.1128/IAI.00136-15
- Brubaker, R.R. Factors promoting acute and chronic diseases caused by Yersinia. Clin. Microbiol. Rev. 1991. Vol. 4. P. 309-324.
- Burrows T.W. Virulence of Pasteurella pestis. Nature, 1957, vol. 179, pp. 1246-1247.
- Busby S., Ebright R.H. Transcription activation by catabolite activator protein (CAP). J. Mol. Biol., 1999, vol. 293, pp. 99-213.
- Butler T., Fu Y.S., Furman L., Almeida C., Almeida A. Experimental Yersinia pestis infection in rodents after intragastric inoculation and ingestion of bacteria. Infect. Immun., 1982, vol. 36, pp. 1160-1167.
- Cavanaugh D.C., Randall R. The role of multiplication of Pasteurella pestis in mononuclear phagocytes in the pathogenesis of fleaborne plague. J. Immunol., 1959, vol. 83, pp. 348-371.
- Charnetzky W.T., Shuford W.W. Survival and growth of Yersinia pestis within macrophages and an effect of the loss of the 47-megadalton plasmid on growth in macrophages. Infect. Immun., 1985, vol. 47, pp. 234-241.
- Chen Y., Duan R., Li X., Li K., Liang J., Liu C., Qiu H., Xiao Y., Jing H., Wang X. Homology analysis and cross-immunogenicity of OmpA from pathogenic Yersinia enterocolitica, Yersinia pseudotuberculosis and Yersinia pestis. Mol. Immunol., 2015, vol. 68, pp. 290-299.
- Corbin B.D., Seeley E.H., Raab A., Feldmann J., Miller M.R., Torres V.J. Metal chelation and inhibition of bacterial growth in tissue abscesses. Science, 2008, vol. 319, pp. 962–965.
- Delcour A. Functon and modulation of bacterial porins: insight from electrophysiology. FEMS Microbiol. Lett., 1997, vol. 151, pp. 115-125.
- Dentovskaia S.V., Kopylov P.Kh., Ivanov S.A., Ageev S.A., Anisimov A.P. A molecular basis of the plague vaccine development. Mol. Gen. Mikrobiol. Virusol., 2013, vol.3, pp. 3-12.
- Dentovskaya S.V., Ivanov S.A., Kopylov P.Kh., Shaikhutdinova R.Z., Platonov M.E., Kombarova T.I., Gapelchenkova T.V., Balakhonov S.V., Anisimov A.P. Selective protective potency of Yersinia pestis ΔnlpD mutants. Acta Naturae, 2015, vol. 7, no. 1, pp. 24.
- Derbise A., Pierre F., Merchez M. Inheritance of the lysozyme inhibitor Ivy was an important evolutionary step by Yersinia pestis to avoid the host innate immune response. J. Infect. Dis., 2013, vol. 207, no. 10, pp. 1535-1543.
- Dintilhac A., Alloing G., Granadel C., Claverys J.P. Competence and virulence of Streptococcus pneumoniae: Adc and PsaA mutants exhibit a requirement for Zn and Mn resulting from inactivation of putative ABC metal permeases. Mol. Microbiol., 1997, vol. 25, pp. 727–739. doi: 10.1046/j.1365-2958.1997.5111879.x
- Dukuzumuremyi J.M., Rosqvist R., Hallberg B., Akerstrom B., Wolf-Watz H., Schesse K. The Yersinia protein kinase A is a host factor inducible RhoA/Rac-binding virulence factor. J Biol. Chem., 2000, vol. 275, no. 45, pp. 35281-35290.
- Erova T.E., Rosenzweig J.A., Sha J., Suarez G., Sierra J.C., Kirtley M.L., van Lier C.J., Telepnev M.V., Motin V.L., Chopra A.K. Evaluation of protective potential of Yersinia pestis outer membrane protein antigens as possible candidates for a new-generation recombinant plague vaccine. Clin. Vaccine Immunol., 2013, vol. 20, no. 2, pp. 227-238.
- Felek S., Jeong J.J., Runco LM., Murray S., Thanassi D.G., Krukonis E.S. Contributions of chaperone/usher systems to cell binding, biofilm formation and Yersinia pestis virulence. Microbiology, 2011, vol. 157, pp. 805-818.
- Felek S., Krukonis E.S. The Yersinia pestis Ail protein mediates binding and Yop delivery to host cells required for plague virulence. Infect. Immun., 2009, vol .77, pp. 825-836.
- Felek S., Lawrenz M.B., Krukonis E.S. The Yersinia pestis autotransporter YapC mediates host cell binding, autoaggregation and biofilm formation. Microbiology, 2008, vol. 154, pp. 1802-1812.
- Felek S., Tsang T.M., Krukonis E.S. Three Yersinia pestis adhesins facilitate Yop delivery to eukaryotic cells and contribute to plague virulence. Infect. Immun., 2010, vol. 78, pp. 4134-4150.
- Feodorova V.A., Corbel M.J. Prospects for new plague vaccines. Expert Rev. Vaccines, 2009, vol. 8, pp. 1721-1738.
- Ferreras J.A., Ryu J.S., Di Lello F., Tan D.S., Quadri L.E. Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat. Chem. Biol., 2005, vol. 1, no. 1, pp. 29-32. doi: 10.1038/nchembio706
- Fong J.C., Yildiz F.H. Interplay between cyclic AMP-cyclic AMP receptor protein and cyclic di-GMP signaling in Vibrio cholerae biofilm formation. J. Bacteriol., 2008, vol. 190, pp. 6646-6659.
- Foote J.W., Delves H.T. Albumin bound and a2 -macroglobulin bound zinc concentrations in the sera of healthy adults. J. Clin. Pathol., 1984, vol. 37, pp. 1050–1054.
- Forman S. Wulff C.R., Myers-Morales T., Cowan C., Perry R.D., Straley S.C. yadBC of Yersinia pestis, a new virulence determinant for bubonic plague. Infect. Immun., 2008, vol. 76, pp. 578-587.
- Fu H., Belaaouaj A.A., Dahlgren C., Bylund J. Outer membrane protein A-deficient Escherichia coli activates neutrophils to produce superoxide and shows increased susceptibility to antibacterial peptides. Microbes Infect., 2003, vol. 5, pp. 781–788.
- Gage K.L., Kosoy M.Y. Natural history of plague: perspectives from more than a century of research. Annu. Rev. Entomol., 2005, vol. 50, pp. 505-528.
- Galindo C.L., Sha J., Moen S.T., Agar S.L., Kirtley M.L., Foltz S.M., McIver L.J., Kozlova E.V., Garner H.R., Chopra A.K. Comparative global gene expression profiles of wild-type Yersinia pestis CO92 and its braun lipoprotein mutant at flea and human body temperatures. Comp. Funct Genomics., 2010. doi: 10.1155/2010/342168.
- Graham A.I., Hunt S., Stokes S.L., Bramall N., Bunch J., Cox A.G. Severe zinc depletion of Escherichia coli: Roles for high-affinity zinc binding by ZinT, zinc transport and zinc-independent proteins. J. Biol. Chem., 2009, vol. 284, pp. 18377–18389.
- Hakansson S., Galyov E.E., Rosqvist R., Wolf-Watz H. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol., 1996, vol. 20, no. 3, pp. 593-603.
- Haneda T., Ishii Y., Danbara H., Okada N. Genome-wide identification of novel genomic islands that contribute to Salmonella virulence in mouse systemic infection. FEMS Microbiol. Lett., 2009, vol. 297, pp. 241-249.
- Hantke K. Bacterial zinc uptake and regulators. Curr. Opin. Microbiol., 2005 vol. 8, pp. 196–202.
- Hantke K., Braun V. Covalent binding of lipid to protein. Diglyceride and amide-linked fatty acid at the N-terminal end of the mureinlipoprotein of the Escherichia coli outer membrane. Eur. J. Biochem., 1973, vol. 34, pp. 284-296.
- Hayashi S., Wu H.C. Lipoproteins in bacteria. J. Bioenerg. Biomembr., 1990, vol. 22, no. 3, pp. 451-71.
- He J., Miyazaki H., Anaya C., Yu F., Yeudall W.A., Lewis J.P. Role of Porphyromonas gingivalis FeoB2 in metal uptake and oxidative stress protection. Infect. Immun., 2006, vol. 74, pp. 4214–4223. doi: 10.1128/IAI.00014-06
- Hinnebusch B.J. Biofilm-dependent and biofilm-independent mechanisms of transmission of Yersinia pestis by fleas. Adv. Exp. Med. Biol., 2012, vol. 954, pp. 237-243.
- Hinnebusch B.J. Transmission factors: Yersinia pestis genes required to infect the flea vector of plague. Adv. Exp. Med. Biol., 2003, vol. 529, pp. 55-62.
- Hinnebusch B.J., Jarrett C.O., Callison J.A., Gardner D., Buchanan S.K., Plano G.V. Role of the Yersinia pestis Ail protein in preventing a protective polymorphonuclear leukocyte response during bubonic plague. Infect. Immun., 2011, vol. 79, pp. 4984-4989.
- Hood M.I., Skaar E.P. Nutritional immunity: transition metals at the pathogen-host interface. Nat. Rev. Microbiol., 2012, vol. 10, pp. 525–537.
- Ichikawa J.K., Li C., Fu J., Clarke S. A gene at 59 minutes on the Escherichia coli chromosome encodes a lipoprotein with unusual amino acid repeat sequences. J. Bacteriol., 1994, vol. 176, pp. 1630-1638.
- Jacob A., Hensley L.K, Safratowich B.D., Quigg R.J., Alexander J.J. The role of the complement cascade in endotoxin-induced septic encephalopathy. Lab. Invest., 2007, vol. 87., pp. 1186-1194.
- Janssen W.A., Surgalla M.J. Plague bacillus: survival within host phagocytes. Science, 1969, vol. 163, no. 3870, pp. 950-952.
- Janulczyk R., Ricci S., Björck L. MtsABC is important for manganese and iron transport, oxidative stress resistance, and virulence of Streptococcus pyogenes. Infect Immun, 2003, vol 71, pp. 2656–2664. doi: 10.1128/IAI.71.5.2656-2664.2003
- Jarrett C.O., Deak E., Isherwood K.E., Oyston P.C., Fischer E.R., Whitney A.R. Transmission of Yersinia pestis from an infectious biofilm in the flea vector. J. Infect. Dis., 2004, vol. 190, no. 4, pp. 783-792.
- Jarrett C.O., Sebbane F., Adamovicz J.J., Andrews G.P., Hinnebusch B.J. Flea-borne transmission model to evaluate vaccine efficacy against naturally acquired bubonic plague. Infect. Immun., 2004, vol. 72, no. 4, pp. 2052-2056.
- Juris S.J., Rudolph A.E., Huddler D., Orth K., Dixon J.E. A distinctive role for the Yersinia protein kinase: actin binding, kinase activation, and cytoskeleton disruption. Proc. Natl. Acad. Sci., 2000, vol. 97, no. 17, pp. 9431-9436.
- Kalivoda E.J., Stella N.A., O’Dee D.M., Nau G.J,, Shanks R.M. The cyclic AMP-dependent catabolite repression system of Serratia marcescens mediates biofilm formation through regulation of type 1 fimbriae. Appl. Environ. Microbiol., 2008, vol. 74, pp. 3461-3470.
- Kehl-Fie T.E., Skaar E.P. Nutritional immunity beyond iron: a role for manganese and zinc. Curr. Opin. Chem. Biol., 2010, vol. 14, pp. 218–224.
- Kehres D.G., Janakiraman A., Slauch J.M., Maguire M.E. SitABCD is the alkaline Mn2+transporter of Salmonella enterica serovar Typhimurium. J. Bacteriol., 2002, vol. 184, pp. 3159–3166. doi: 10.1128/JB.184.12.3159-3166.2002
- Kim T.J., Chauhan S., Motin V.L., Goh E.B., Igo M.M., Young G.M. Direct transcriptional control of the plasminogen activator gene of Yersinia pestis by the cyclic AMP receptor protein. J. Bacteriol., 2007, vol. 189, pp. 8890-8900.
- Kim W.K., Jang P.G., Woo M.S., Han I.O., Piao H.Z., Lee K., Lee H., Joh T.H., Kim H.S. A new anti-inflammatory agent KL-1037 represses proinflammatory cytokine and inducible nitric oxide synthase (iNOS) gene expression in activated microglia. Neuropharmacology, 2004, vol. 47, no. 2, pp. 243-252.
- Kolodziejek A.M., Schnider D.R., Rohde H.N., Wojtowicz A.J., Bohach G.A., Minnich S.A., Hovde C.J. Outer membrane protein X (Ail) contributes to Yersinia pestis virulence in pneumonic plague and its activity is dependent on the lipopolysaccharide core length. Infect. Immun., 2010, vol. 78, pp. 5233-5243.
- Kolodziejek A.M., Sinclair D.J., Seo K.S., Schnider D.R., Deobald C.F., Rohde H.N., Viall A.K., Minnich S.S., Hovde C.J., Minnich S.A., Bohach G.A. Phenotypic characterization of OmpX, an Ail homologue of Yersinia pestis KIM. Microbiology, 2007, vol. 153, pp. 2941-2951.
- Kopylov P.Kh., Platonov M.E., Ablamunits V.G., Kombarova T.I., Ivanov S.A., Kadnikova L.A., Somov A.N., Dentovskaya S.V., Uversky V.N., Anisimov A.P. Yersinia pestis Caf1 Protein: Effect of Sequence Polymorphism on Intrinsic Disorder Propensity, Serological Cross-Reactivity and Cross-Protectivity of Isoforms. PLoS One, 2016, vol. 11, no. 9, e0162308. doi: 10.1371/journal.pone.0162308
- Lange R., Hengge-Aronis R. The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation. Mol. Microbiol., 1994, vol. 13, no. 4, pp. 733-743.
- Lathem W.W., Price P.A., Miller V.L., Goldman W.E. A plasminogen-activating protease specifically controls the development of primary pneumonic plague. Science, 2007, vol. 15, pp. 509-513.
- Lathem W.W., Schroeder J.A., Bellows L.E., Ritzert J.T., Koo J.T., Price P.A. Posttranscriptional regulation of the Yersinia pestis cyclic AMP receptor protein Crp and impacton virulence. M. Bio., 2014, vol. 5, e01038-13.
- Lawrenz M.B., Lenz J.D., Miller V.L. A novel autotransporter adhesin is required for efficient colonization during bubonic plague. Infect. Immun., 2009, vol. 77, pp. 317-326.
- Lawrenz M.B., Pennington J., Miller V.L. Acquisition of OmpT in reveals cryptic virulence function of autotransporter YapE in Yersinia pestis. Mol. Microbiol., 2013, vol. 89, pp. 276-287.
- Lazar S.W., Kolter R. SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol., 1996, vol. 178, pp. 1770-1773.
- Lee K., Gao Y., Yao Z.J., Phan J., Wu L., Liang J., Waugh D.S., Zhang Z.Y., Burke T.R.Jr. Tripeptide inhibitors of Yersinia protein-tyrosine phosphatase. Bioorg. Med. Chem. Lett., 2003, vol. 13, no. 15, pp. 2577-81.
- Lee V.T., Schneewind O. Type III machines of pathogenic yersiniae secrete virulence factors into the extracellular milieu. Mol. Microbiol., 1999, vol. 31, pp. 1619-1629.
- Lenz J.D., Temple B.R., Miller V.L. Evolution and virulence contributions of the autotransporter proteins YapJ and YapK of Yersinia pestis CO92 and their homologs in Y. pseudotuberculosis IP32953. Infect. Immun., 2012, vol. 80, pp. 3693-3705.
- Letzelter M., Sorg I., Mota LJ., Meyer S., Stalder J., Feldman M. The discovery of SycO highlights a new function for type III secretion effector chaperones. EMBO J., 2006, vol. 25, no. 13, pp. 3223-3233.
- Li B., Guo J., Wang X., Ni B., Ke Y., Zhu Z., Guo Z., Yang R. High-throughput identification of new protective antigens from a Yersinia pestis live vaccine by enzyme-linked immunospot assay. Infect. Immun., 2009, vol. 77, no. 10, pp. 4356-4361.
- Lim K.H.L., Jones C.E., vanden Hoven R.N., Edwards J.L., Falsetta M.L., Apicella M.A., Jennings M.P., McEwan A.G. Metal binding specificity of the MntABC permease of Neisseria gonorrhoeae and its influence on bacterial growth and interaction with cervical epithelial cells. Infect. Immun., 2008, vol. 76, pp. 3569–3576. doi: 10.1128/IAI.01725-07
- Lin J.S., Szaba F.M., Kummer L.W., Chromy B.A., Smiley S.T. Yersinia pestis YopE Contains a Dominant CD8 T Cell Epitope that Confers Protection in a Mouse Model of Pneumonic Plague. J. Immunol., 2011, vol. 187, no 2, pp. 897–904. doi: 10.4049/jimmunol.1100174
- Liu F., Chen H., Galván E.M., Lasaro M.A., Schifferli D.M. Effects of Psa and Cаf1 on the adhesive and invasive interactions of Yersinia pestis with human respiratory tract epithelial cells. Infect Immun., 2006, vol. 74, pp. 5636-5644.
- Liu H., Wang H., Qiu J., Wang X., Guo Z., Qiu Y. Transcriptional profiling of a mice plague model: insights into interaction between Yersinia pestis and its host. J. Basic Microbiol., 2009, vol. 49, no. 1, pp. 4992-4999.
- Liu L., Fang H., Yang H., Zhang Y., Han Y., Zhou D., Yang R. CRP is an activator of Yersinia pestis biofilm formation that operates via a mechanism involving gmhA and waaAE-coaD. Front. Microbiol., 2016, vol. 7.
- Liuzzi J.P., Lichten L.A., Rivera S., Blanchard R.K., Aydemir T.B., Knutson M.D. Interleukin-6 regulates the zinc transporter Zip14 in liver and contributes to the hypozincemia of the acute-phase response. Proc. Natl. Acad. Sci. USA, 2005, vol. 102, pp. 6843–6848.
- Llobet E., March C., Giménez P., Bengoechea J.A. Klebsiella pneumoniae OmpA confers resistance to antimicrobial peptides. Antimicrob. Agents Chemother., 2009, vol. 53, pp. 298-302.
- Lorange E.A., Race B.L., Sebbane F., Hinnebusch B.J. Poor vector competence of fleas and the evolution of hypervirulence in Yersinia pestis. J. Infect. Dis., 2005, vol. 191, no. 11, pp. 1907-1912.
- Lu X.H., An S.Q., Tang D.J., McCarthy Y., Tang J.L., Dowetal J.M. RsmA regulates biofilm formation in Xanthomonas campestris through a regulatory network involving cyclicdi-GMP and the Clp transcription factor. PLoS ONE, 2012, vol. 7, e52646.
- Marra A., Lawson S., Asundi J.S., Brigham D., Hromockyj A.E. In vivo characterization of the psa genes from Streptococcus pneumoniae in multiple models of infection. Microbiology, 2002, vol. 148, pp. 1483–1491.
- McKelvie J.C., Richards M., Harmer J.E., Milne T.S., Roach P.L., Oyston P.C. Inhibition of Yersinia pestis DNA adenine methyltransferase in vitro by a stibonic acid compound: identification of a potential novel class of antimicrobial agents. Br. J. Pharmacol., 2013, vol. 168, no. 1, pp 172-88. doi: 10.1111/j.1476-5381.2012.02134.x
- Melching L., Vas S.I. Effects of serum components on gram-negative bacteria during bactericidal reactions. Infect. Immun., 1971, vol. 3, pp. 107-115.
- Murphy B.S., Wulff C.R., Garvy B.A., Straley S.C. Yersinia pestis YadC: a novel vaccine candidate against plague. Adv. Exp. Med. Biol., 2007, vol. 603, pp. 400-414.
- Navarro L., Koller A., Nordfelth R., Wolf-Watz H., Taylor S., Dixon J.E. Identification of a molecular target for the Yersinia protein kinase A. Mol. Cell., 2007, vol. 26, pp. 465-477.
- Neilsen P.O., Zimmerman G.A., McIntyre T.M. Escherichia coli Braun lipoprotein induces a lipopolysaccharide-like endotoxic response fromprimary human endothelial cells. J. Immunol., 2001, vol. 167, pp. 5231-5239.
- Nordfelth R., Kauppi A.M., Norberg H.A., Wolf-Watz H., Elofsson M. Small-molecule inhibitors specifically targeting type III secretion. Infect. Immun., 2005, vol. 73, no. 5, pp. 3104-14. doi: 10.1074/jbc.M413122200
- Obi I.R., Francis M.S. Demarcating SurA activities required for outer membrane targeting of Yersinia pseudotuberculosis adhesions. Infect. Immun., 2013, vol. 81, pp. 2296-2308.
- Obi I.R., Nordfelth R., Francis M.S. Varying dependency of periplasmic peptidylprolyl cis-transisomerases in promoting Yersinia pseudotuberculosis stress tolerance and pathogenicity. Biochem. J., 2011, vol. 439, pp. 321-332.
- Oh M.H., Lee S.M, Lee D.H., Choi S.H. Regulation of the Vibrio vulnificus hupA gene by temperature alteration and cyclic AMP receptor protein and evaluation of its role in virulence. Infect. Immun., 2009, vol. 77, pp. 1208-1215.
- Ouyang Z., He M., Oman T., Yang X.F., Norgard M.V. A manganese transporter, BB0219 (BmtA), is required for virulence by the Lyme disease spirochete, Borrelia burgdorferi. Proc. Natl. Acad. Sci. USA, 2009, vol. 106, pp. 3449–3454. doi: 10.1073/pnas.0812999106
- Paik S., Brown A., Munro C. L., Cornelissen C. N., Kitten T. The sloABCR operon of Streptococcus mutans encodes an Mn and Fe transport system required for endocarditis virulence and its Mn-dependent repressor. J. Bacteriol., 2003, vol. 185, pp. 5967–5975. doi: 10.1128/JB.185.20.5967-5975.2003
- Park H., Teja K., O'Shea J.J., Siegel R.M. The Yersinia effector protein YpkA induces apoptosis independently of actin depolymerization. J. Immunol., 2007, vol. 178, no. 10, pp. 6426-6434.
- Park J.S., Lee E.J., Lee J.C., Kim W.K., Kim H.S. Anti-inflammatory effects of short chain fatty acids in IFN-gamma-stimulated RAW 264.7 murine macrophage cells: involvement of NF-kappaB and ERK signaling pathways. Int. Immunopharmacol., 2007, vol. 7, pp. 70-77.
- Parkhill J., Wren B.W., Thomson N.R. Genome sequence of Yersinia pestis, the causative agent of plague. Nature, 2001, vol. 413, pp. 523-527.
- Perry R.D., Abney J., Mier I. Jr., Lee Y., Bearden S.W., Fetherston J.D. Regulation of the Yersinia pestis Yfe and Ybt iron transport systems. Adv. Exp. Med. Biol., 2003, vol. 529, pp. 275–283. doi: 10.1007/0-306-48416-1_53
- Perry R.D., Craig S.K., Abney J., Bobrov A.G., Kirillina O., Mier I. Jr., Truszczynska H., Fetherston J.D. Manganese transporters Yfe and MntH are Fur-regulated and important for the virulence of Yersinia pestis. Fur. Microbiology, 2012, vol. 158, pp. 804–815. doi: 10.1099/mic.0.053710-0
- Perry R.D., Fetherston J.D. Yersinia pestis - etiologic agent of plague. Clin. Microbiol. Rev., 1997, vol. 10, no. 1, pp. 35-66.
- Perry R.D., Shah J., Bearden S.W., Thompson J.M., Fetherston J.D. Yersinia pestis TonB: role in iron, heme, and hemoprotein utilization. Infect. Immun., 2003, vol. 71, no. 7, pp. 4159-4162.
- Petersen S., Young G.M. Essential role for cyclic AMP and its receptor protein in Yersinia enterocolitica virulence. Infect. Immun., 2002, vol. 70, pp. 3665-3672.
- Petrarca P., Ammendola S., Pasquali P., Battistoni A. The Zur-regulated ZinT protein is an auxiliary component of the high-affinity ZnuABC zinc transporter that facilitates metal recruitment during severe zinc shortage. J. Bacteriol., 2010, vol. 192, pp. 1553–1564.
- Philipovskiy A.V., Smiley S.T. Vaccination with live Yersinia pestis primes CD4 and CD8 T cells that synergistically protect against lethal pulmonary Y. pestis infection. Infect Immun. 2007, vol.75, no 2, pp. 878–885. doi: 10.1128/IAI.01529-06
- Ponnusamy D., Fitts E.C., Sha J., Erova T.E., Kozlova E.V., Kirtley M.L. High-throughput, signature-tagged mutagenic approach to identify novel virulence factors of Yersinia pestis CO92 in a mouse model of infection. Infect. Immun., 2015, vol. 83, pp. 2065–2081. doi: 10.1128/IAI.02913-14
- Prasadarao N.V., Wass C.A, Weiser J.N., Stins M.F., Huang S.H. Kim K.S Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells. Infect. Immun., 1996, vol. 64, pp. 146-153.
- Prehna G., Ivanov M.I., Bliska J.B., Stebbins C.E. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell, 2006, vol. 126, no. 5, pp. 869-880.
- Pujol C., Grabenstein J.P., Perry R.D., Bliska J.B. Replication of Yersinia pestis in interferon-(-activated macrophages requires ripA, a gene encoded in the pigmentation locus. PNAS, 2005, vol. 102, no. 36, pp. 12909-12914.
- Quenee L.E., Schneewind O. Plague vaccines and the molecular basis of immunity against Yersinia pestis. Hum. Vaccin., 2009, vol. 5, pp. 817-823.
- Rahuel-Claremont S., Dunn M.F. The biological chemistry of zinc. In: Rainsford K.D., Milanino R., Sorenson R.J., Velo G.P., editors. Copper and Zinc in Inflammatory and Degenerative Diseases. Kluwer Academic Publisher, 1998. pp. 47–59.
- Rickman L., Scott C., Hunt D.M, Hutchinson T., Menendez M.C., Whalan R. A member of the cAMP receptor protein family of transcription regulatorsin Mycobacterium tuberculosis is required for virulence in mice and controls transcription of the rpfA gene coding for a resuscitation promoting factor. Mol. Microbiol., 2005, vol. 56, pp. 1274-1286.
- Rink L., Haase H. Zinc homeostasis and immunity. Trends Immunol., 2007, vol. 28, pp. 1–4.
- Roediger W.E. Nitric oxide-dependent nitrosation of cellular CoA: a proposal for tissue responses. Nitric. Oxide, 2001, vol. 5, no. 2, pp. 83-87.
- Roediger W.E., Babidge W.J. Nitric oxide effect on colonocyte metabolism: co-action of sulfides and peroxide. Mol. Cell Biochem., 2000, vol. 206, no. 1-2, PP. 159-167.
- Roggenkamp A., Ackermann N., Jacobi C.A., Truelzsch K., Hoffmann H., Heesemann J. Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA. Journal of bacteriology, 2003, vol. 185, pp. 3735-3744.
- Rouviere P.E., Gross C.A. SurA, a periplasmic protein with peptidyl-prolylisomerase activity, participates in the assembly of outer membrane porins. Genes Dev., 1996, vol. 10, pp. 3170-3182.
- Runco L.M, Myrczek S., Bliska J.B., Thanassi D.G. Biogenesis of the fraction 1 capsule and analysis of the ultrastructure of Yersinia pestis. J Bacteriol., 2008, vol. 190, pp. 3381-3385.
- Salazar J.K., Wu Z., Yang W., Freitag N.E., Tortorello M.L., Wang H. Roles of an ovel Crp/Fnr family transcription factor Lmo0753 in soil survival, biofilm production and surface attachment of resh produce of Listeria monocytogenes. PLoS ONE, 2013, vol. 8, e75736.
- Santiviago C.A., Reynolds M.M., Porwollik S., Choi S.H., Long F. Analysis of pools of targeted Salmonella deletion mutants identifies novel genes affecting fitness during competitive infection in mice. PLoS Pathog., 2009, vol. 5, e1000477.
- Schubot F.D., Cherry S., Austin B.P., Tropea J.E., Waugh D.S. Crystal structure of the protease-resistant core domain of Yersinia pestis virulence factor YopR. Protein Sci., 2005, vol. 14, pp. 1679-1683.
- Senior N.J., Sasidharan K., Saint R.J., Scott A.E., Sarkar-Tyson M., Ireland P.M., Bullifent H.L., Rong Yang Z., Moore K., Oyston P.C.F., Atkins T.P., Atkins H.S., Soyer O.S., Titball R.W. An integrated computational-experimental approach reveals Yersinia pestis genes essential across a narrow or a broad range of environmental conditions. BMC Microbiol., 2017, vol. 17, no. 1, pp. 163. doi: 10.1186/s12866-017-1073-8
- Seo K.S., Kim J.W., Park J.Y., Viall A.K., Minnich S.S., Rohde H.N. Role of a new intimin/invasin-like protein in Yersinia pestis virulence. Infect. Immun., 2012, vol. 80, pp. 3559-3569.
- Sha J., Agar L.S., Baze W.B., Olano J.P., Fad A.A., Erova T.E., Wang S., Foltz S.M., Suarez G., Motin V.L., Chauhan S., Klimpel G.R., Peterson J.W., Chopra A.K. Braun Lipoprotein (Lpp) Contributes to Virulence of Yersiniae: Potential Role of Lpp in Inducing Bubonic and Pneumonic Plague. Infection and Immunity, 2008, vol. 76, no. 4, pp. 1390-1409.
- Sha J., Kirtley L.M., van Lier C. J., Wang S., Erova T.E., Kozlova E.V., Cao A., Cong Y., Fitts E. C., Rosenzweig J.A., Chopra A.K. Deletion of the Braun Lipoprotein-Encoding Gene and Altering the Function of Lipopolysaccharide Attenuate the Plague Bacterium. Infection and Immunity, 2013, vol. 81, pp. 815-828.
- Shi L., Adkins J.N., Coleman J.R., Schepmoes A.A., Dohnkova A. Proteomic analysis of Salmonella enterica serovar typhimurium isolated from RAW 264.7 macrophages: identification of a novel protein that contributes to the replication of serovar typhimurium inside macrophages. J. Biol. Chem., 2006, vol. 281, pp. 29131-29140.
- Simonet M., Riot B., Fortineau N., Berche P. Invasin production by Yersinia pestis is abolished by insertion of an IS200-like element within the inv gene. Infect. Immun, 1996, vol. 64, pp. 375-379.
- Skorupski K., Taylor R.K. Cyclic AMP and its receptor protein negatively regulate the coordinate expression of cholera toxin and toxin- coregulated pilusin Vibrio cholerae. Proc. Natl. Acad. Sci., 1997, vol. 94, pp. 265-270.
- Smiley S.T. Immune defense against pneumonic plague. Immunol. Rev., 2008, vol. 225, pp. 256-271.
- Smith A.J., Ward P.N., Field T.R., Jones C.L., Lincoln R.A., Leigh J.A. MtuA, a lipoprotein receptor antigen from Streptococcus uberis, is responsible for acquisition of manganese during growth in milk and is essential for infection of the lactating bovine mammary gland. Infect. Immun., 2003, vol. 71, pp. 4842–4849. doi: 10.1128/IAI.71.9.4842-4849.2003
- Sohnle P.G., Hunter Michael J., Hahn B., Chazin Walter J.. Zinc reversible antimicrobial activity of recombinant calprotectin (migration inhibitory factor - related proteins 8 and 14). J. Infect. Dis., 2000, vol. 182, pp. 1272–1275.
- Southern S.J., Scott A.E., Jenner D.C., Ireland P.M., NorvilleI H., Sarkar-Tyson M. Survival protein A is essential for virulence in Yersinia pestis. Microbial Pathogenesis, 2016, vol. 92, pp. 50-53.
- Straley S.C., Harmon P.A. Growth in mouse peritoneal macrophages of Yersinia pestis lacking established virulence determinants. Infection and immunity, 1984, vol. 45, no. 3, pp. 649-654.
- Sugawara E., Nikaido H. Pore-forming activity of OmpA protein of Escherichia coli. J. Biol. Chem., 1992, vol. 267, pp. 2507-2511.
- Sun Y.C., Guo X.P., Hinnebusch B.J., Darby C. The Yersinia pestis Rcs phosphorelay inhibits biofilm formation by repressing transcription of the diguanylate cyclase gene hmsT. J. Bacteriol., 2012, vol. 194, no. 8, pp. 2020-2026.
- Sun Y.C., Hinnebusch B.J., Darby C. Experimental evidence for negative selection in the evolution of Yersinia pestis pseudogene. Proc. Nat. Acad. Sci., 2008, vol. 105, no. 23, pp. 8097-8101.
- Sun Y.C., Jarrett C.O., Bosio C.F., Hinnebusch B.J. Retracing the evolutionary path that led to flea-borne transmission of Yersinia pestis. Cell Host Microbe, 2014, vol. 15, no. 5, pp. 578-586.
- Suzuki H., Nishimura Y., Yasuda S., Nishimura A., Yamada M., Hirota Y. Murein-lipoprotein of Escherichia coli: a protein involved in the stabilization of bacterial cell envelope. Molecular and General Genetics, 1978, vol. 167, no. 1, pp. 1-9.
- Tautz L., Bruckner S., Sareth S., Alonso A., Bogetz J., Bottini N., Pellecchia M., Mustelin T. Inhibition of Yersinia Tyrosine Phosphatase by Furanyl Salicylate Compounds. J. Biol. Chem., 2005, vol. 280, no. 10, pp. 9400-8. doi: 10.1074/jbc.M413122200
- TidharA., Flashner Y., Cohen S., Levi Y., Zauberman A., Gur D., Aftallon M., Elhanany E., Zvi A., Shafferman A., Mamroud E. The NlpD lipoprotein is a novel Yersinia pestis virulence factor essential for the development of plague. PLoS One, 2009, vol. 4: e7023.
- Titball R.W., Williamson E.D. Yersinia pestis (plague) vaccines. Expert. Opin. Biol. Ther., 2004, vol. 4, pp. 965-973.
- Tormo A., Almiron M., Kolter R. SurA, an Escherichia coli gene essential for survival in stationary phase. J. Bacteriol., 1990, vol. 172, pp. 4339-4347.
- Torres R., Chim N., Sankaran B., Pujol C., Bliska J., Gouldinga C.W. Structural insights into RipC, a putative citrate lyase b subunit from a Yersinia pestis virulence operon. Acta. Cryst., 2012, vol. 68, pp. 2-7.
- Torres R., Lan B., Latif Y., Chima N., Goulding C.W. Structural snapshots along the reaction pathway of Yersinia pestis RipA, a putative butyryl-CoA transferase. Acta. Cryst., 2014, vol. 70, pp. 1074-1085.
- Torres R., Swift R.V., Chim N., Wheatley N., Lan B., Atwood B.R., Pujol C., Sankaran B., Bliska J.B., Amaro R.E., Goulding C.W. Biochemical, structural and molecular dynamics analyses of the potential virulence factor RipA from Yersinia pestis. PLoS ONE, 2011, vol. 6, I. 9, e25084.
- Torres-Escobar A., Juarez-Rodriguez M.D., Lamont R.J., Demuth D.R. Transcriptional regulation of Aggregatibacter actinomycetemcomitans lsrACDBFG and lsrRK operons and their role in biofilm formation. J. Bacteriol., 2013, vol. 195, pp. 56-65.
- Trasak C., Zenner G., Vogel A., Yuksekdag G., Rost R., Haase I. Yersinia protein kinase YopO is activated by a novel G-actin binding process. J. Biol. Chem. 2007, vol. 282, no. 4, pp. 2268-2277.
- Tsang T.M., Felek S., Krukonis E.S. Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery. Infect. Immun., 2010, vol. 78, pp. 3358-3368.
- van Lier С.J., Tiner B.L., Chauhan S., Motin V.L., Fitts E.C., Huante M.B., Endsley J.J., Ponnusamy D., Sha J., Chopra A.K. Further characterization of a highly attenuated Yersinia pestis CO92 mutant deleted for the genes encoding Braun lipoprotein and plasminogen activator protease in murine alveolar and primary human macrophages. Microb. Pathog., 2015, vol. 80, pp. 27-38.
- Wang S., Joshi S., Mboudjeka I., Liu F., Ling T., Goguen J.D., Lu S. Relative immunogenicity and protection potential of candidate Yersinia pestis antigens against lethal mucosal plague challenge in Balb/C mice. Vaccine, 2008, vol. 26, pp. 1664-1674.
- Weening E.H., Cathelyn J.S., Kaufman G., Lawrenz M.B., Price P., Goldman W.E., Miller V.L. The dependence of the Yersinia pestis capsule on pathogenesis is influenced by the mouse background. Infect. Immun., 2011, vol. 79, no. 2, pp. 644.
- Weinberg E.D. Infectious diseases influenced by trace element environment. Ann. NY Acad. Sci., 1972, vol. 199, pp. 274–284.
- Wiley D.J., Nordfeldth R., Rosenzweig J., DaFonseca C.J., Gustin R., Wolf-Watz H. The Ser/Thr kinase activity of the Yersinia protein kinase A (YpkA) is necessary for full virulence in the mouse, mollifying phagocytes, and disrupting the eukaryotic cytoskeleton. Microb. Pathog., 2006, vol. 40, no. 5, pp. 234-243.
- Willias S.P., Chauhan S., Lo C.C., Chain P.S., Motin V.L. CRP-mediated carbon catabolite regulation of Yersinia pestis biofilm formation is enhanced by the carbon storage regulator protein, CsrA. PLoS ONE, 2015, vol. 10, e0135481.
- Yen Y.T., Karkal A., Bhattacharya M., Fernandez R.C., Stathopoulos C. Identification and characterization of autotransporter proteins of Yersinia pestis KIM. Mol. Membr. Biol., 2007, vol. 24, pp. 28-40.
- Zhan L., Han Y., Yang L., Geng J., Li Y., Gao H. The cyclic AMP receptor protein, CRP, is required for both virulence and expression of the minimal CRP regulon in Yersinia pestis biovar Microtus. Infect. Immun., 2008, vol. 76, pp. 5028-5037.
- Zhan L., Yang L., Zhou L., Li Y., Gao H., Guo Z. Direct and negative regulation of the sycO-ypkA-ypoJ operon by cyclic AMP receptor protein (CRP) in Yersinia pestis. BMC Microbiol., 2009, vol. 9, pp. 178.
- Zhang H.J., Peterson J.W., Niesel D.W., Klimpel G.R. Bacterial lipoprotein and lipopolysaccharide act synergistically to induce lethal shock and proinflammatory cytokine production. J. Immunol., 1997, vol. 159, pp. 4868-4878.
- Zhang Y., Wang L., Han Y., Yan Y., Tan Y., Zhou L. Autoregulation of PhoP/PhoQ and positive regulation of the cyclic AMP receptor protein-cyclic AMP complex by PhoP in Yersinia pestis. J. Bacteriol., 2013, vol. 195, pp. 1022-1030.
- Zvi A., Rotem Sh., Zauberman A., Elia U., Aftalion M., Bar-Haim E., Mamroud E., Cohen O. Novel CTL epitopes identified through a Y. pestis proteome-wide analysis in the search for vaccine candidates against plague. Vaccine, 2017, vol. 35, no. 44, pp. 5995-6006