BINDING OF COLLAGEN, FIBRONECTIN, LACTOFERRIN, LAMININ, VITRONECTIN AND HEPARAN-SULFATE TO STAPHYLOCOCCUS-AUREUS STRAIN-V8 AT VARIOUS GROWTH PHASES AND UNDER NUTRIENT STRESS CONDITIONS

Citation
Od. Liang et al., BINDING OF COLLAGEN, FIBRONECTIN, LACTOFERRIN, LAMININ, VITRONECTIN AND HEPARAN-SULFATE TO STAPHYLOCOCCUS-AUREUS STRAIN-V8 AT VARIOUS GROWTH PHASES AND UNDER NUTRIENT STRESS CONDITIONS, Zentralblatt fur Bakteriologie, 279(2), 1993, pp. 180-190
Citations number
39
Categorie Soggetti
Microbiology,Virology
ISSN journal
09348840
Volume
279
Issue
2
Year of publication
1993
Pages
180 - 190
Database
ISI
SICI code
0934-8840(1993)279:2<180:BOCFLL>2.0.ZU;2-H
Abstract
We have examined how Staphylococcus aureus strain V8 cells interact wi th I-125-labelled extracellular matrix (ECM) and serum proteins (colla gen type I and IV), fibronectin, lactoferrin, laminin, vitronectin, an d heparan sulphate at various phases of the growth cycle. Maximal bind ing of these glycoproteins and heparan sulphate to the bacteria occurr ed after 17 to 20 h in the late stationary phase except for fibronecti n-binding, which was maximal after 12 to 14 h. Binding of the glycopro teins and heparan sulphate to S. aureus V8 under nutrient stress condi tions exhibited complex patterns based on different starving condition s and various binding ligands. In general, bacteria starved in distill ed water and 0.02 M potassium phosphate buffer (pH 7.2) at room temper ature showed high susceptibility to all binding ligands within the fir st 18 h, followed by entering a lower binding period (except for colla gen-binding which still remained high). The binding was not correlated to cell surface charge or hydrophobicity of the bacteria. Furthermore , extracellular and cell-associated proteolytic activity of starved ce lls against ECM and serum proteins was found to be greater than for no n-starved cells. Thus, S. aureus could sustain its ability to bind var ious connective tissue and cell surface components during a long perio d of time even in the absence of energy-yielding substrates.