Activity of Catabolic Enzymes of Film-Forming Strains of Staphylococcus aureus

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Abstract:

The activity of glucose catabolism pathways of staphylococci strains able to form biofilm and isolated from vagina of women with dysbiosis of reproductive tract and strains isolated 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 reproductive tract dysbiosis, 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 inhibit 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.

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[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.

DOI: 10.1099/mic.0.27865-0

Google Scholar

[2] H.F. Chambers, The changing epidemiology of Staphylococcus aureus, Emerg. Infect. Dis. 7 (2001) 178–182.

DOI: 10.3201/eid0702.010204

Google Scholar

[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.

DOI: 10.1016/0005-2728(67)90050-3

Google Scholar

[4] E. Hofmann, G. Kopperschläger, Phosphofructokinase from yeast, Methods in Enzymology. 90 (1982) 49–60.

Google Scholar

[5] V.L. Crow, G.G. Pritchard, Pyruvate kinase from Streptococcus lactis, Methods in Enzymology. 90 (1982) 165–170.

DOI: 10.1016/s0076-6879(82)90122-7

Google Scholar

[6] J. Everse, Enzymic determination of lactic acid, Methods in Enzymology. 41 (1975) 41–44.

DOI: 10.1016/s0076-6879(75)41011-4

Google Scholar

[7] U. Dobrindt et al., Genomic islands in pathogenic and environmental microorganisms, Nat. Rev. Microbiol. 2 (2004) 414–424.

DOI: 10.1038/nrmicro884

Google Scholar

[8] F. Götz, Staphylococci in colonization and disease: prospective targets for drugs and vaccines, Curr. Opin. Microbiol. 7 (2004) 477–487.

DOI: 10.1016/j.mib.2004.08.014

Google Scholar

[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.

DOI: 10.1016/s1570-0232(02)00907-8

Google Scholar

[10] J.G. Holt et al. (Eds.), Bergey's manual of determinative bacteriology, Williams & Wilkins, Baltimore, 1994.

Google Scholar

[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.

Google Scholar

[12] About the unification of microbiological (bacteriological) research methods used in clinical diagnostic laboratories of medical institutions: the order № 535, MOZ USSR, Moscow, 1985.

Google Scholar

[13] M.K. Roberts, The diagnosis of staphylococcal infection, Mir, Moscow, Russia, 2005. (in Russian)

Google Scholar

[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.

DOI: 10.1016/0005-2728(70)90247-1

Google Scholar

[15] S. Ujita, K. Kimura, Fructose-1,6-bisphosphate aldolase from Bacillus subtilis, Methods in Enzymology. 90 (1982) 235–241.

DOI: 10.1016/s0076-6879(82)90132-x

Google Scholar

[16] L. Kletsova et al., Glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Methylobacillus flagellatum, Methods in Enzymology. 188 (1990) 335–339.

DOI: 10.1016/0076-6879(90)88052-c

Google Scholar

[17] R. Bridges, C. Wittenberger, 6-Phosphogluconate dehydrogenase from Streptococcus faecalis, Methods in Enzymology. 41 (1975) 232–237.

DOI: 10.1016/s0076-6879(75)41053-9

Google Scholar

[18] G.A. Kochetov, Transketolase from yeast, rat liver, and pig liver, Methods in Enzymology. 90 (1982) 209–223.

DOI: 10.1016/s0076-6879(82)90128-8

Google Scholar