Activity of catabolic enzymes of film-forming strains of Staphylococcus aureus

• Autorzy: Voronkova O.S. , Shevchenko T.M. , Vinnikov A.I.
• Języki publikacji: EN

Abstrakty

EN

The activity of glucose catabolism pathways of film-forming strains of staphylococci isolated from vagina of women with dysbiosis of reproductive tract and from women without disorders of microflora was studied. It was established that the investigated film-forming strains utilized the carbohydrates by pentose phosphate pathway mainly, as indicated by 23-33% higher enzyme activity compare to strains isolated from healthy women. Instead strains, isolated from women without dysbiosis of reproductive tract, have higher activity of glycolytic enzymes on 13- 28%. The prevalence of glycolytic transformation of glucose by strains isolated from healthy women also indicates by the depression of glucose oxidation during action of monoiodinacetate – classical inhibitor of glycolysis. It inhibits glycolysis of strains isolated from healthy women more significant. It was established that oxidase activity of film-forming strains isolated from women with dysbiosis, increased over 40% during the use of basic substrates of citric acid cycle. These data indicate a general increase of catabolic activity of oxidative type of staphylococci isolated during vaginal dysbiosis and able to form biofilm.

Słowa kluczowe

EN

Staphylococcus aureus; bacterial strain; biofilm formation; catabolic enzyme; metabolic process; oxidase activity; dysbacteriosis

• Wydawca: -
• Czasopismo: International Letters of Natural Sciences
• Rocznik: 2017
• Tom: 61
• Opis fizyczny: p.8-13,ref.

Twórcy

autor

Voronkova O.S.

• Oles Honchar Dnipropetrovsk National University, Gagarin av.72, Dnipro, Ukraine

autor

Shevchenko T.M.

• Oles Honchar Dnipropetrovsk National University, Gagarin av.72, Dnipro, Ukraine

autor

Vinnikov A.I.

• Oles Honchar Dnipropetrovsk National University, Gagarin av.72, Dnipro, Ukraine

Bibliografia

• [1] M.A. Tormo et al., Bap-dependent biofilm formation by pathogenic species of Staphylococcus: evidence of horizontal gene transfer, Microbiology. 151 (2005) 2465–2475.
• [2] H.F. Chambers, The changing epidemiology of Staphylococcus aureus, Emerg. Infect. Dis. 7 (2001) 178–182.
• [3] U.A. Cole, J.M.T. Wimpenny, D.E Hughes, The ATP pool in Escherichia coli. I. Measurement of the pool using a modifies luciferase assay, Biochimica et Biophysica Acta (BBA)-Bioenergetics. 143(3) (1967) 445–453.
• [4] E. Hofmann, G. Kopperschläger, Phosphofructokinase from yeast, Methods in Enzymology. 90 (1982) 49–60.
• [5] V.L. Crow, G.G. Pritchard, Pyruvate kinase from Streptococcus lactis, Methods in Enzymology. 90 (1982) 165–170.
• [6] J. Everse, Enzymic determination of lactic acid, Methods in Enzymology. 41 (1975) 41–44.
• [7] U. Dobrindt et al., Genomic islands in pathogenic and environmental microorganisms, Nat. Rev. Microbiol. 2 (2004) 414–424.
• [8] F. Götz, Staphylococci in colonization and disease: prospective targets for drugs and vaccines, Curr. Opin. Microbiol. 7 (2004) 477–487.
• [9] M. Hecker, S. Engelmann, S.J. Cordwell, Proteomics of Staphylococcus aureus – current state and future challenges, Journal of Chromatography. 787(1) (2003) 179–195.
• [10] J.G. Holt et al. (Eds.), Bergey’s manual of determinative bacteriology, Williams & Wilkins, Baltimore, 1994.
• [11] I.I. Volkov, Improving the microbiological diagnosis of staphylococcal infections and environmental aspects of their pathogens, 1999. Information on http://nature.web.ru/db/msg.html?mid=1163020.
• [12] About the unification of microbiological (bacteriological) research methods used in clinical diagnostic laboratories of medical institutions: the order № 535, MOZ USSR, Moscow, 1985.
• [13] M.K. Roberts, The diagnosis of staphylococcal infection, Mir, Moscow, Russia, 2005. (in Russian)
• [14] W.P. Hempling Studies on the efficiency of oxidative phosphorylation in intact Escherichia coli B, Biochimica et Biophysica Acta (BBA)-Bioenergetics. 205(2) (1970) 169–182.
• [15] S. Ujita, K. Kimura, Fructose-1,6-bisphosphate aldolase from Bacillus subtilis, Methods in Enzymology. 90 (1982) 235–241.
• [16] L. Kletsova et al., Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Methylobacillus flagellatum, Methods in Enzymology. 188 (1990) 335–339.
• [17] R. Bridges, C. Wittenberger, 6-Phosphogluconate dehydrogenase from Streptococcus faecalis, Methods in Enzymology. 41 (1975) 232–237.
• [18] G.A. Kochetov, Transketolase from yeast, rat liver, and pig liver, Methods in Enzymology. 90 (1982) 209–223.

Identyfikatory

DOI

10.18052/www.scipress.com/ILNS.61.8