PERSISTENCE OF STREPTOCOCCUS PYOGENES
- Authors: Dmitrieva N.F1, Timofeev Y.M1, Briko N.I1
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Affiliations:
- Sechenov Moscow Medical Academy, Russia
- Issue: Vol 86, No 3 (2009)
- Pages: 104-109
- Section: Articles
- Submitted: 13.06.2023
- Published: 15.06.2009
- URL: https://microbiol.crie.ru/jour/article/view/14241
- ID: 14241
Cite item
Full Text
Abstract
State-of-the-art data on persistence of Streptococcus pyogenes are presented. Survival and persistence of S.pyogenes in organism of the host are considered as a result of action of widely presented virulent functions of infectious agent aimed on evasion from defense mechanisms of the host. Information on adhesins, bacteriocins, IgA-proteases, molecules with invasive function, as well as with function of protection from pahocytosis is presented. Antigenic mimicry and L-forms of S.pyogenes are briefly characterized.
About the authors
N. F Dmitrieva
Sechenov Moscow Medical Academy, Russia
Yu. M Timofeev
Sechenov Moscow Medical Academy, Russia
N. I Briko
Sechenov Moscow Medical Academy, Russia
References
- Бородиюк Н.А., Дробышевская Э.И., Басиновский Л.В. и др. Изучение узкой специфичности моноклональных антител, направленных к разным детерминантам полисахарида стрептококка группы А. Иммунология. 1993, 4: 47—49.
- Брико Н.И., Дмитриева Н.Ф., Ещина А.С. и др. Носительство СГА: новые данные по характеристике биологии возбудителя и иммунного ответа. Журн. микробиол. 1994, приложение: 51—55.
- Бухарин О.В. Персистенция патогенных бактерий. М., Медицина, 1999.
- Бухарин О.В., Усвяцов Б.Я., Карташова О.Л. Биология патогенных кокков. М., Медицина, 2002.
- Горина Л.Г., Вульфович Ю.В. Дифференциация антигенов циркулирующих иммунных комплексов. Журн. микробиол. 1996, 1: 58—61.
- Дмитриева Н.Ф., Тимофеев Ю.М., Брико Н.И. Липотейхоевые и тейхоевые кислоты патогенных стрептококков: структура, функции, роль во взаимодействии возбудителя с макроорганизмом. Там же. 2007, 6: 100—107.
- Ермолина Л.М. Острая ревматическая лихорадка. Хронические ревматические болезни сердца. М., 2006.
- Казеева Т.Н., Шевелев А.Б. IgA-специфичные белки патогенных бактерий. Биохимия. 2009, 74 (1): 17—29.
- Костюкова Н.Н. Микробиологические факторы, определяющие носительство при капельных инфекциях. Журн. микробиол. 1997, 4: 10—15.
- Обгольц А.А. Механизмы персистирования бактерий. Там же. 1992, 4: 70—72.
- Покровский В.И., Брико Н.И., Ряпис Л.А. Стрептококки и стрептококкозы. М., 2006.
- Савельев Е.П., Дмитриева Н.Ф., Дынга Л.О. Аутолитическое расщепление клеточных стенок стрептококка группы А. Вестн. АМН СССР. 1986, 4 (7): 27—30.
- Тотолян А.А. Патогенность стрептококков и ее молекулярные и генетические механизмы. Л., Наука, 1988.
- Шихман А.Р., Чернякова А.М., Брико Н.И. Персистенция и биодеградация клеточных стенок стрептококков группы А в свете иммунопатогенеза негнойных постстрептококковых заболеваний. Журн. микробиол. 1990, 2: 74—79.
- Aziz R.K., Kotb M. Rise and persistence of global M1T1 clone of Streptococcus pyogenes. Emerg. Infect. Dis. 2008, 14 (10): 1511—1517.
- Baird R.W., Courtney H.S., Bronze M.S. et al. Passiv protection against group A streptococcal infection in mice by lipoteichoic acid. Clin. Res. 1999, 38: 353—357.
- Burova L., Schalen C., Gladilina M. Antigenic diversity of IgG Fc-receptors in Streptococcus pyogenes. In: T.Horaud et al. (ed.). Streptococci and the host. N.Y., Plenum. Press., 1997, p. 585—587.
- Cue D., Dombek P.E., Lam H. And Cleary P.P. Streptococcus pyogenes serotype M1 encodes multiple pathways for entry into human epithelial cells. Infect. Immun. 1998, 66: 4593—4601.
- Cunningham M.W. Pathogenesis of group A streptococcal infections. Ibid. 2000, 13 (3): 470—564.
- Eriksson A., Norgren M. Cleavage of antigen-bound immunoglobulin G by SpeB contributes to streptococcal persistence in opsonizing blood. Ibid. 71 (1): 211—217.
- Fischetty V. Streptococcal M-protein: molecular design and biological behavior. Clin. Microbiol. 1989, 2: 285—314.
- Gillen C., Courtney H., Schulze K. et al. Opacity factor activity and epithelial cell binding by the serum opacity factor protein of Streptococcus pyogenes are functionally discrete. J. Biol. Chem. 2008, 283: 6359—6366.
- Hanski E., Caparon M. Protein F., fibronectin-binding protein is an adhesin of group A Streptococcus.Proc. Natl. Acad. Sci. USA. 1992: 89: 6172—6176.
- Heng N.C., Burtenshaw G.A., Jack R.W. et al. Sequence analysis of pDN571, a plasmid encoding novel bacteriocin production in M-type 57 Streptococcus pyogenes. Plasmid. 2004, 52 (3): 225—229.
- Hoe N.P., Ireland R.M., DeLeo F.R. et al. Insight into the molecular basis of pathogen abundance: group A Streptococcus inhibitor of complement inhibits bacterial adherence and internalization into human cells. Proc. Natl. Acad. Sci. USA. 2002, 99 (11): 7646—7651.
- Husmann L.K., Yung D-L., Hollingshead S.K. et al. Role of putative factors of Streptococcus pyogenes in mouse models of long-term throat colonization and pneumonia. Infect. Immun. 1997, 65: 1422—1430.
- Jadoun J.,Burstein E., Hanski E., Sela S. Proteins M6 and F1 are required for efficient invasion of group A streptococci into cultured epithelial cells. In: T. Horaud et al. (ed.). Streptococci and the host. New York, Plenum. Press, 1997, c. 511—515.
- Klenk M., Nakata M., Podbielski A. et al. Streptococcus pyogenes serotype-dependent and independent changes in infected HEp-2 epithelial cells. ISME J. 2007 1 (8): 678—692.
- La Penta D., Rubens C., Chi E.,Cleary P.P. Group A streptococci efficiently invade human respiratory epithelial cells. Proc. Natl. Acad. Sci. USA. 1994. 91: 12115—12119.
- Lee J., Caparon M. An Oxygen-Induced but Protein F- Independent Fibronectin-Binding Pathway in Streptococcus pyogenes. Infect. Immun.1996, 64 (2): 413—421.
- Lee S., Mitchell D., Hensler M. Discovery of widely distributed toxin biosynthetic gene cluster. Proc. Natl. Acad. Sci. USA. 2008, 105 (15): 5879—5884.
- Medina E., Goldmann O., Toppel A.W. et al. Survival of Streptococcus pyogenes within host phagocytic cells: a pathogenic mechanism for persistence and systemic invasion. J. Infect. Dis. 2003,187 (4): 597—603.
- Medina E., Rohde M., Gursharan S. Intracellular survival of Streptococcus pyogenes in polymorphonuclear cells results in increased bacterialvirulence. Infect. Immun. 2003,71 (9): 5376—5380.
- Molinari G., Rohde M., Talay S.R. The role played by the group A streptococcal negative regulator Nra on bacterial interactions with epithelial cells. Mol. Microbiol. 2001, 40 (1): 99—105.
- Molinari G., Talay S.R., Valentin-Weigand P. et al. The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells. Infect. Immun. 1997, 65: 1357—1363.
- Ofek I., Simpson W.A., Beachey E.H. Formation of molecular complexes between a structurally defind M-protein and acylated or deacylated lipoteichoic acid of Streptococcus pyogenes. J. Bacteriol. 1982, 149: 426—432.
- Okada N., Liszewski M., Atkinson J., Caparon M. Membrane cofactor protein (CD46) is keratinocyte receptor for the M protein of the group A Streptococcus. Proc. Natl. Acad. Sci. USA. 1995, 92: 2489—2493.
- Oliver M.A., García-Rey C., Bosch R. et al. Evaluation of the ability of erythromycin-resistant and- susceptible pharyngeal group A Streptococcus isolates from Spain to enter and persist in human keratinocytes. J. Med. Microbiol. 2007, 56 (11): 1485—1489.
- Osterlund A., Engstrand L. Intracellular penetration and survival of Streptococcus pyogenes in respiratory epithelial cells in vitro. Acta Otolaryngol. (Stockholm). 1995, 115: 685—688.
- Osterlund A., Popa R., Nikkila T. et al. Intracellular reservoir of Streptococcus pyogenes in vivo: a possible explanationfor recurrent pharyngotonsillitis. Laringoscopc. 1997, 107: 640—646.
- Podbielski A., Kreikemeyer B. Persistence of group A streptococci in eukaryotic cells-a safe place? Lancet. 2001, 358 (9275): 3—4.
- Podbielski A. Flexible architecture of the Streptococcus pyogenes FCT genome region: finally the clue for understanding purulent skin diseases and long-term persistence. J. Bacteriol. 2007, 189 (4): 1181—1184.
- Shockman G.D., Holtje J.V. Microbial peptidoglycan (murein) hydrolases. Ibid. 1988, 170: 1783—1788.
- Smith H. The revival of interest in mechanisms of bacterial pathogenicity. Biol.Rev. 1995, 70: 277—316.
- Spinaci C., Magi G., Varaldo P.E. et al. Persistence of erythromycin-resistant group a streptococci in cultured respiratory cells. Pediatr. Infect. Dis. J. 2006, 25 (10): 880—883.
- Stockbauer K.E., Maagoun L., Liu M. et al. A natural variant of the cysteine protease virulence factor of group A Streptococcus with an arginine-glicine-aspartic acid (RGD) motif preferentially binds human integrins. Proc. Natl. Acad. Sci. USA. 1998, 95: 3128—3133.
- Tylewska S.K., Fischetti V.A., Gibbons R.J. Binding selectivity of Streptococcus pyogenes and M-protein to epithelial cells differs from that of lipoteichoic acid. Curr. Microbiol. 1988, 16: 209—216.
- Voyich J., Sturdevant E., Braughton K. Genome-wide protective responce used by group A Streptococcus to evade destruction by human polymorphonuclear leucocytes. Proc. Natl. Acad. Sci. USA. 2003, 100: 1996—2001.
- Wessels M.R., Bronze M.S. Role of hyaluronic acid capsule in pharingeal colonisation and invasive infection by group A streptococcus. Pathogene streptococcii, present and future. St. Pet., 1994.
- Wood D.N., Chaussee M.A., Chaussee M.S. et al. Persistence of Streptococcus pyogenes in stationaryphase cultures. J. Bacteriol. 2005, 187 (10): 3319—3328.