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