Binding of extracellular matrix proteins by lactobacilli.
Ten gut and ten vaginal Lactobacillus strains were investigated for their ability to bind type I collagen (Cn-I) and four selected gut lactobacilli were investigated for their binding to other extracellular matrix (ECM) molecules. Immobilized Cn-I (100 mg/L) in wells of microtitre plates was bound by all 10 autoaggregating vaginal strains and by 3 strains of gut lactobacilli from piglets in the range of A570 readings 0.114-1.806. L. acidophilus strain SV31 was much more adherent than the rest of strains. All four gut lactobacilli tested for binding to other ECM molecules displayed good binding to porcine fibronectin and heparin and some of them bound weakly to fetuin and porcine mucin. No binding of these strains was observed to bovine mucin, bovine fibrinogen and bovine lactoferrin.
Styriak
I
I
Institute of Animal Physiology, Slovak Academy of Sciences, 040 01 Kosice, Slovakia.
Zatkovic
B
B
Marsalková
S
S
D000818:Animals; D002417:Cattle; D003094:Collagen / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005260:Female; D007778:Lactobacillus / Q000378:metabolism*; D013270:Stomach / Q000382:microbiology; D013552:Swine; D014621:Vagina / Q000382:microbiology
D016326:Extracellular Matrix Proteins; D003094:Collagen