Журнал микробиологии, эпидемиологии и иммунобиологии. 2016; : 94-101
ХИТИНОЛИТИЧЕСКИЙ КОМПЛЕКС VIBRIO CHOLERAE: СОСТАВ И РОЛЬ В ПЕРСИСТЕНЦИИ
Дуванова О. В., Мишанькин Б. Н., Романова Л. В., Титова С. В.
https://doi.org/10.36233/0372-9311-2016-5-94-101Аннотация
Список литературы
1. Дуванова О.В., Мишанькин Б.Н., Водопьянов А.С., Сорокин В.М. N-ацетил-β-D-глюкозаминидаза холерных вибрионов. Журн. микробиол. 2016, 2: 41-48.
2. Дуванова О.В., Мишанькин Б.Н., Сорокин В.М., Титова С.В.Оценка влияния температуры культивирования на активность N-ацетил-β-D-глюкозаминидазы у холерных вибрионов. ЗНиСО, 2016, 4 (277): 42-44.
3. Журавлева Н.В., Лукьянов П.А. Хитинолитические ферменты: источники, характеристика и применение в биотехнологии. Вестник ДВО РАН. 2004, 3: 76-86.
4. Ильина А.В., Варламов В.П., Тихонов В.Е., Ямсков И.А., Даванков В.А. Выделение высокоочищенной хитиназы Streptomyces kurssanovii на модифицированном хитине. Биотехнология.1992,2: 25-28.
5. Малеев В.В., Особо опасные микозы. Волгоград, Волга-Паблишер, 2013.
6. Мишанькин Б.Н., Романова Л.В., Ломов Ю.М., Шиманюк Н. Я., Водопьянов С.О., Черепахина И.Я., Сучков И.Ю., Дуванова О.В. Vibrio cholera 0139, выделенные от людей и из воды открытых водоемов. Журн. микробиол. 2000, 3: 3-7.
7. Мишанькин Б.Н., Шиманюк Н.Я., Водопьянов С.О., Романова Л.В., Водопьянов А.С., Дуванова О.В., Атарова Г.Т., Демьяненко С.В. Изучение хитинолитического комплекса холерного вибриона сероварианта 0139. Биотехнология. 2010, 1: 32-40.
8. Скрябин К.Г. Хитин и хитозан. Получение, свойства и применение. Москва, Наука, 2002.
9. Стояченко И.А., Варламов В.П. Очистка и некоторые свойства хитиназ из Streptomyces kurssanovii. Биотехнология. 1992, 2: 29-36.
10. Amako К., Shimodori S., Imoto T. et al. Effects of chitin and its soluble derivatives on survival of Vibrio cholerae Ol at low temperature. Appl. Environm. Microbiol. 1987, 3 (53), 603-605.
11. Appleby L.J., Nausch N., Bourke C.D. Chitinase 3-like 1 protein levels are elevated in Schistosoma haematobium infected children. PLoS Negl. Trop. Dis. 2012, 11 (6): e. 1898, doi: 10.1371.
12. Bassler B.L., Gibbons P.J., Yu C. et al. Chitin utilization by marine bacteria. Chemotaxis to chitin oligosaccharides by Vibrio fumissii. J. Biol. Chem.1991. 36 (266): 24268-24275.
13. Bohr S., Petel S.J., Vasko R. et al. The role CHI3L1 (Chitinase 3-like-1) in the pathogenesis of infections in burns in a mouse model. PloS One. 2015, 11 (10): e.0140440. doi: 10137.
14. Colwell R. Global climate and infectious diseases: the cholera paradigm. Science. 1996, 274: 2025-2031.
15. Davis B., Eveleigh D. Chitosanases: occurrence, production and immobilization. Chitin, chitosan and related enzymes. Ed. Zikakis J.P. Orlando. Academic Press, 1984, p. 161-179.
16. Dela Cruz C.S., Lu W., He C.H. et al. Chitinase 3-like-l promotes Streptococcus pneumoniae killing and augments host tolerance to lung antibacterial responses. Cell Host Microbe. 2012, 1:34-46.
17. Di Rosa M., Distefano G., Zorena K. Chitinases and immunity: ancestral molecules with new functions. Immunobioology. 2016, 3 (221): 399-411.
18. Hunt D. E., Gevers D., Vahora N. M. et al. Conservation of the chitin utilization pathway in the Vibrionaceae. Appl. Environ. Microbiol. 2008, 1 (74): 44-51.
19. Kaneko T., Colwell R.R. Adsorption of Vibrio parahaemolyticus onto chitin and zooplank-tonic copepods. Appl. Microbiol. 1975, 29: 251-257.
20. Kaplan J.B., Ragunath C., Velliyagounder K. et al. Enzymatic detachment of Staphylococcus epidermidis biofilms. Antimicrob Agents Chemotherap. 2004, 7 (48): 2633-2636.
21. Keyhani N. O., Roseman S. Physiological aspects of chitin catabolism in marine bacteria. Biochim. Biophys. Acta. 1999, 1473: 108-122.
22. Keyhani N. O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio fumissii. Molecular cloning, isolation and characterization of the periplasmic chitodextrinase. J. Biol. Chem. 1996, 52 (271): 33414-33424.
23. Kobayashi T, Koide O., Deguchi S. et al. Characterization of chitosanase of a deep biosphere Bacillus strain. Biosci. Biotechnol. Biochem. 2011, 4 (75), 669-673.
24. Li X., Roseman S., Morita K., Fukumoto I. et al. The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and two-component chitin catabolic sensor/kinase. Proc.Natl. Acad. Sci. USA. 2004, 2 (101): 627-631.
25. Lipp E. K., Huq A., Colwell R. R. Effect ofglobal climate on infectious diseases: the cholera model. Clin. Microbiol. Rev. 2002, 15: 757-770.
26. Lo Scrudato M., Blokesch M. The regulatory network of natural competence and transformation of Vibrio cholerae. PLoS Genet. 2012, 6: el002778.
27. Low D., Subramaniam R., Aomatsu T. et al. Chitinase 3-like-l induces survival and proliferation of intestinal epithelial cells during chronic inflammation and colitis-associated cancer by regulating S100A9. Oncotarget. 2015, 34 (6): 3635-3650.
28. Low D., Tran H.T., DreuxN. et al. Chitin-binding domains of Escherichia coli ChiA mediate interactions with intestinal epithelial cells in mice with colits. Gastroenterology. 2013, 3 (145): 602-612.
29. Ma B., Herzog E.L., Lee C.G. et al. Role of chitinase 3-like-l and semaphoring 7a in pulmonary melanoma metastasis. Cancer Res. 2015, 3 (75): 487-496.
30. Meibom K. L., Li X. B., Nielsen A. T. et al. The Vibrio cholerae chitin utilization program. Proc. Soc. Acad. Sci. USA. 2004, 8 (101): 2524-2529.
31. Moiler H. Grelier S., Pardon P. et al. Antimicrobial and physicochemical properties ofchitosan - HPMC - based films. J. Agric. Food Chem. 2004, 52: 6585-6591.
32. Nalin D. R., Daya V, Reid A. Adsorption and growth of Vibrio cholerae on chitin. Infect. Immun. 1979, 2 (25): 768-770.
33. Park J. K., Yamasaki Y., Nakagawa T. et al. Purification and characterization of the chitinase (ChiA) from Enterobacter sp. G-l. Biosci. Biotechnol. Biochem. 1997, 61: 684-689.
34. Patil S. R., Ghormade V, Deshpande M. V Chitinolytic enzymes: an exploration. Enzyme Microb. Technol. 2000, 26: 473-483.
35. Rabea E. J., Badawy M., StevensC. V. et al. Chitosan as antimicrobial agents: Application and mode action. Biomacromolecules 2003, 6 (4): 1457-1465.
36. Reguera G., Kolter R. Virulence and environment: a novel role for Vibrio cholerae toxin-coregulated pili in biofilm formation on chitin. J. Bacteriol. 2005, 10 (187): 3551-3555.
37. Reimann L., Azam F. Widespread N-acetyl-D-glucosamine uptake among pelagic marine bacteria and its ecological implications. App. Environ. Microbiol. 2002, 68: 5554-5562.
38. Rinaudo M. Chitin and chitosan: Properties and applications. Prog. Polym. Sci. 2006, 31: 603-632.
39. Sahai A.S., Manocha M.S. Chitinases of fungi and plants: their involvement in morphogenesis and host parasite interaction. FEMS Microbiol. Rev. 1993, 11: 317-338.
40. Sikora A.E. Proteins secreted via the type II secretion system: smart strategies of Vibrio cholerae to maintain fitness in different ecological niches. PLoS pathogens. 2013, 2 (9): e 1003126. doi: 10.137.
41. Sun S., Tay S., Kjelleberg S.A. et al. Quorum sensing-regulated chitin metabolism provides grazing resistance to Vibrio cholerae biofdms. IS ME J. 2015, 9 (8): 1812-1820.
42. Taira T., Ohnuma T, Yamagami T. et al. Antifungal activity of rye (Secale cereale) seed chiti-nases: the different binding manner of class I and class II chitinases to the fungal cell wall. Biosci. Biotechnol. Biochem. 2002, 66: 970-977.
43. Tamayo R., Patimalla B., Camilli A. Growth in biofilm induces a hyperinfections phenotype in Vibrio cholerae. Infect. Immun. 2010, 78 (8): 3560-3569.
44. Tarsi R., Pruzzo C. Role of surface proteins in Vibrio cholerae attachment to chitin. Appl. Env. Microbiol. 1999, 3 (66): 1348-1351.
45. Tran H.T., Bamich N., Mizoguchi E. Potential role of chitinase and chitin-binding proteins in host-microbial interactions during the development of intestinal inflammation. Elistol Histopathol. 2011, 11 (26): 1453-1464.
46. Varnum S. M., Webb-Robertson B. J., Moore R.J. et al. Proteomic analysis of broncoalveolar lavage fluid proteins from mice infected with Francisella tularensis ssp.novicida. J.Proteome Res. 2012, 7 (11): 3690-3703.
47. Watve S. S., Thomas J., Hammer В. K. CytR is global positive regulator of competence, type VI secretion, and chitinases in Vibrio cholerae. PLoS One. 2015,10 (9): eO 138834.eCollection 2015.
48. Yamamoto S., Izumiya H., Mitobe J. et al. Identification of a chitin-induced small RNAthat regulates translation of the tfoX gene, encoding a positive regulator of natural competence in Vibrio cholerae. J. Bacteriol. 2011, 8 (193): 1953-1965.
Journal of microbiology, epidemiology and immunobiology. 2016; : 94-101
VIBRIO CHOLERAE CHITINOLYTIC COMPLEX: THE COMPOSITION AND THE ROLE IN PERSISTANCE
Duvanova O. V., Mishankin B. N., Romanova L. V., Titova S. V.
https://doi.org/10.36233/0372-9311-2016-5-94-101Abstract
References
1. Duvanova O.V., Mishan'kin B.N., Vodop'yanov A.S., Sorokin V.M. N-atsetil-β-D-glyukozaminidaza kholernykh vibrionov. Zhurn. mikrobiol. 2016, 2: 41-48.
2. Duvanova O.V., Mishan'kin B.N., Sorokin V.M., Titova S.V.Otsenka vliyaniya temperatury kul'tivirovaniya na aktivnost' N-atsetil-β-D-glyukozaminidazy u kholernykh vibrionov. ZNiSO, 2016, 4 (277): 42-44.
3. Zhuravleva N.V., Luk'yanov P.A. Khitinoliticheskie fermenty: istochniki, kharakteristika i primenenie v biotekhnologii. Vestnik DVO RAN. 2004, 3: 76-86.
4. Il'ina A.V., Varlamov V.P., Tikhonov V.E., Yamskov I.A., Davankov V.A. Vydelenie vysokoochishchennoi khitinazy Streptomyces kurssanovii na modifitsirovannom khitine. Biotekhnologiya.1992,2: 25-28.
5. Maleev V.V., Osobo opasnye mikozy. Volgograd, Volga-Pablisher, 2013.
6. Mishan'kin B.N., Romanova L.V., Lomov Yu.M., Shimanyuk N. Ya., Vodop'yanov S.O., Cherepakhina I.Ya., Suchkov I.Yu., Duvanova O.V. Vibrio cholera 0139, vydelennye ot lyudei i iz vody otkrytykh vodoemov. Zhurn. mikrobiol. 2000, 3: 3-7.
7. Mishan'kin B.N., Shimanyuk N.Ya., Vodop'yanov S.O., Romanova L.V., Vodop'yanov A.S., Duvanova O.V., Atarova G.T., Dem'yanenko S.V. Izuchenie khitinoliticheskogo kompleksa kholernogo vibriona serovarianta 0139. Biotekhnologiya. 2010, 1: 32-40.
8. Skryabin K.G. Khitin i khitozan. Poluchenie, svoistva i primenenie. Moskva, Nauka, 2002.
9. Stoyachenko I.A., Varlamov V.P. Ochistka i nekotorye svoistva khitinaz iz Streptomyces kurssanovii. Biotekhnologiya. 1992, 2: 29-36.
10. Amako K., Shimodori S., Imoto T. et al. Effects of chitin and its soluble derivatives on survival of Vibrio cholerae Ol at low temperature. Appl. Environm. Microbiol. 1987, 3 (53), 603-605.
11. Appleby L.J., Nausch N., Bourke C.D. Chitinase 3-like 1 protein levels are elevated in Schistosoma haematobium infected children. PLoS Negl. Trop. Dis. 2012, 11 (6): e. 1898, doi: 10.1371.
12. Bassler B.L., Gibbons P.J., Yu C. et al. Chitin utilization by marine bacteria. Chemotaxis to chitin oligosaccharides by Vibrio fumissii. J. Biol. Chem.1991. 36 (266): 24268-24275.
13. Bohr S., Petel S.J., Vasko R. et al. The role CHI3L1 (Chitinase 3-like-1) in the pathogenesis of infections in burns in a mouse model. PloS One. 2015, 11 (10): e.0140440. doi: 10137.
14. Colwell R. Global climate and infectious diseases: the cholera paradigm. Science. 1996, 274: 2025-2031.
15. Davis B., Eveleigh D. Chitosanases: occurrence, production and immobilization. Chitin, chitosan and related enzymes. Ed. Zikakis J.P. Orlando. Academic Press, 1984, p. 161-179.
16. Dela Cruz C.S., Lu W., He C.H. et al. Chitinase 3-like-l promotes Streptococcus pneumoniae killing and augments host tolerance to lung antibacterial responses. Cell Host Microbe. 2012, 1:34-46.
17. Di Rosa M., Distefano G., Zorena K. Chitinases and immunity: ancestral molecules with new functions. Immunobioology. 2016, 3 (221): 399-411.
18. Hunt D. E., Gevers D., Vahora N. M. et al. Conservation of the chitin utilization pathway in the Vibrionaceae. Appl. Environ. Microbiol. 2008, 1 (74): 44-51.
19. Kaneko T., Colwell R.R. Adsorption of Vibrio parahaemolyticus onto chitin and zooplank-tonic copepods. Appl. Microbiol. 1975, 29: 251-257.
20. Kaplan J.B., Ragunath C., Velliyagounder K. et al. Enzymatic detachment of Staphylococcus epidermidis biofilms. Antimicrob Agents Chemotherap. 2004, 7 (48): 2633-2636.
21. Keyhani N. O., Roseman S. Physiological aspects of chitin catabolism in marine bacteria. Biochim. Biophys. Acta. 1999, 1473: 108-122.
22. Keyhani N. O., Roseman S. The chitin catabolic cascade in the marine bacterium Vibrio fumissii. Molecular cloning, isolation and characterization of the periplasmic chitodextrinase. J. Biol. Chem. 1996, 52 (271): 33414-33424.
23. Kobayashi T, Koide O., Deguchi S. et al. Characterization of chitosanase of a deep biosphere Bacillus strain. Biosci. Biotechnol. Biochem. 2011, 4 (75), 669-673.
24. Li X., Roseman S., Morita K., Fukumoto I. et al. The chitinolytic cascade in Vibrios is regulated by chitin oligosaccharides and two-component chitin catabolic sensor/kinase. Proc.Natl. Acad. Sci. USA. 2004, 2 (101): 627-631.
25. Lipp E. K., Huq A., Colwell R. R. Effect ofglobal climate on infectious diseases: the cholera model. Clin. Microbiol. Rev. 2002, 15: 757-770.
26. Lo Scrudato M., Blokesch M. The regulatory network of natural competence and transformation of Vibrio cholerae. PLoS Genet. 2012, 6: el002778.
27. Low D., Subramaniam R., Aomatsu T. et al. Chitinase 3-like-l induces survival and proliferation of intestinal epithelial cells during chronic inflammation and colitis-associated cancer by regulating S100A9. Oncotarget. 2015, 34 (6): 3635-3650.
28. Low D., Tran H.T., DreuxN. et al. Chitin-binding domains of Escherichia coli ChiA mediate interactions with intestinal epithelial cells in mice with colits. Gastroenterology. 2013, 3 (145): 602-612.
29. Ma B., Herzog E.L., Lee C.G. et al. Role of chitinase 3-like-l and semaphoring 7a in pulmonary melanoma metastasis. Cancer Res. 2015, 3 (75): 487-496.
30. Meibom K. L., Li X. B., Nielsen A. T. et al. The Vibrio cholerae chitin utilization program. Proc. Soc. Acad. Sci. USA. 2004, 8 (101): 2524-2529.
31. Moiler H. Grelier S., Pardon P. et al. Antimicrobial and physicochemical properties ofchitosan - HPMC - based films. J. Agric. Food Chem. 2004, 52: 6585-6591.
32. Nalin D. R., Daya V, Reid A. Adsorption and growth of Vibrio cholerae on chitin. Infect. Immun. 1979, 2 (25): 768-770.
33. Park J. K., Yamasaki Y., Nakagawa T. et al. Purification and characterization of the chitinase (ChiA) from Enterobacter sp. G-l. Biosci. Biotechnol. Biochem. 1997, 61: 684-689.
34. Patil S. R., Ghormade V, Deshpande M. V Chitinolytic enzymes: an exploration. Enzyme Microb. Technol. 2000, 26: 473-483.
35. Rabea E. J., Badawy M., StevensC. V. et al. Chitosan as antimicrobial agents: Application and mode action. Biomacromolecules 2003, 6 (4): 1457-1465.
36. Reguera G., Kolter R. Virulence and environment: a novel role for Vibrio cholerae toxin-coregulated pili in biofilm formation on chitin. J. Bacteriol. 2005, 10 (187): 3551-3555.
37. Reimann L., Azam F. Widespread N-acetyl-D-glucosamine uptake among pelagic marine bacteria and its ecological implications. App. Environ. Microbiol. 2002, 68: 5554-5562.
38. Rinaudo M. Chitin and chitosan: Properties and applications. Prog. Polym. Sci. 2006, 31: 603-632.
39. Sahai A.S., Manocha M.S. Chitinases of fungi and plants: their involvement in morphogenesis and host parasite interaction. FEMS Microbiol. Rev. 1993, 11: 317-338.
40. Sikora A.E. Proteins secreted via the type II secretion system: smart strategies of Vibrio cholerae to maintain fitness in different ecological niches. PLoS pathogens. 2013, 2 (9): e 1003126. doi: 10.137.
41. Sun S., Tay S., Kjelleberg S.A. et al. Quorum sensing-regulated chitin metabolism provides grazing resistance to Vibrio cholerae biofdms. IS ME J. 2015, 9 (8): 1812-1820.
42. Taira T., Ohnuma T, Yamagami T. et al. Antifungal activity of rye (Secale cereale) seed chiti-nases: the different binding manner of class I and class II chitinases to the fungal cell wall. Biosci. Biotechnol. Biochem. 2002, 66: 970-977.
43. Tamayo R., Patimalla B., Camilli A. Growth in biofilm induces a hyperinfections phenotype in Vibrio cholerae. Infect. Immun. 2010, 78 (8): 3560-3569.
44. Tarsi R., Pruzzo C. Role of surface proteins in Vibrio cholerae attachment to chitin. Appl. Env. Microbiol. 1999, 3 (66): 1348-1351.
45. Tran H.T., Bamich N., Mizoguchi E. Potential role of chitinase and chitin-binding proteins in host-microbial interactions during the development of intestinal inflammation. Elistol Histopathol. 2011, 11 (26): 1453-1464.
46. Varnum S. M., Webb-Robertson B. J., Moore R.J. et al. Proteomic analysis of broncoalveolar lavage fluid proteins from mice infected with Francisella tularensis ssp.novicida. J.Proteome Res. 2012, 7 (11): 3690-3703.
47. Watve S. S., Thomas J., Hammer V. K. CytR is global positive regulator of competence, type VI secretion, and chitinases in Vibrio cholerae. PLoS One. 2015,10 (9): eO 138834.eCollection 2015.
48. Yamamoto S., Izumiya H., Mitobe J. et al. Identification of a chitin-induced small RNAthat regulates translation of the tfoX gene, encoding a positive regulator of natural competence in Vibrio cholerae. J. Bacteriol. 2011, 8 (193): 1953-1965.
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