The interactions between spiral and coccoid forms, extracellular matrix (ECM) and plasma proteins were studied in an I-labelled protein assay. The range of binding of collagen V, plasminogen, human lactoferrin (HLf) and vitronectin to coccoid forms of NCTC 11637 was 26–48%. In contrast, binding of radiolabelled fibronectin and collagen types I and III was low (3–8%). The coccoid forms of 14 strains of showed significant HLf binding (median 26%). With plasminogen, no significant difference was found between binding to the coccoid (median = 13%) and spiral (median = 12%) forms, of 13 of the 14 strains of tested; the exception was strain NCTC 11637. I-plasminogen showed a dose-dependent binding to both the coccoid and spiral forms. Plasminogen binding to both forms was specific; the binding was inhibited by non-labelled plasminogen, plasmin, lysine, EACA (epsilon-aminocaproic acid) but not by fetuin or various carbohydrates. Similarly, HLf binding was found to be specific and was inhibited by non-labelled HLf and BLf. The coccoid forms showed either similar or enhanced ECM binding capabilities compared with the spiral forms. As the binding of ECM proteins may be an important mechanism of tissue adhesion for various pathogenic bacteria, the coccoid differentiated form of can be considered as an infective form in the pathogenesis of helicobacter infection and type B gastritis.


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