Mode of Binding of Fibrinogen, Fibronectin and Iron-binding Proteins by Animal Enterococci

Veterinary Research Communications, 28 (2004) 587^598

# 2004Kluwer Academic Publishers. Printed in the NetherlandsMode of Binding of Fibrinogen, Fibronectin and Ironbinding Proteins by Animal EnterococciI. Styriak1*, A. Laukova1, V. Strompfova1 and A. Ljungh21Institute of Animal Physiology, Slovak Academy of Sciences, Soltesovej 4-6, 040 01

Kosice, Slovakia;2Department of Medical Microbiology, Dermatology and Infection,

Lund University, Sweden*Correspondence: E-mail: [email protected], I., Laukova, A., Strompfova,V.and Ljungh,A., 2004. Mode of binding of brinogen, bronectin

and iron-binding proteins by animal enterococci. Veterinary Research Communications, 28(7), 587^598ABSTRACTSixty-two animal enterococci were examined for their binding of bovine brinogen, porcine bronectin,

bovine lactoferrin, bovine apotransferrin and human holotransferrin in the particle agglutination assay

(PAA). Individual strains expressed binding of selected glycoproteins to various degrees (0, 1, 2, 3),

whereas bovine brinogen binding of enterococci from goats, rabbits and rodents was the strongest (3)

in general. Porcine bronectin was bound weakly (1 or 2) by enterococci from horses, dogs, poultry,

rabbits and rodents, while most of the goat isolates and half of the dog feed isolates did not bind

bronectin (0). Bovine lactoferrin was bound especially by the isolates from rodents and rabbits. Bovine

apotransferrin was bound very weakly (1) by only a few isolates. Human holotransferrin was bound to a

greater extent than apotransferrin by some isolates from rabbits and rodents. Since multiresistant

strains are preferred in our binding studies, enterococci were also examined for their antibiotic

resistance pattern. Almost all investigated isolates were resistant at least to one antibiotic. However,

some strains displayed resistance to ve or six antibiotics of 10 antibiotics tested. In a study of the

inhibitory eect of heparin, porcine mucin and hyaluronic acid, the greatest eect was observed after

heparin treatment of bacterial cells. These observations, as well as the expression of heparin binding by

most strains, may suggest that at least one mode of enterococcal attachment utilizes glycosaminoglycan

chains present on the surface of adherent cells.Keywords: Enterococcus, extracellular matrix, brinogen, bronectin, lactoferrin, transferrin, heparinAbbreviations: ECM, extracellular matrix; Fn, bronectin; GAGs, glycosaminoglycans; Lf, lactoferrin;

MSCRAMM, microbial surface components recognizing adhesive matrix molecules; PAA, particle

agglutination assay; tDNA-PCR, tRNA intergenic spacer PCR; Tf, transferrinINTRODUCTIONEnterococci are members of the normal intestinal ora and are found in the faeces of

most healthy humans and animals. Over the last decade, enterococci have emerged...