BINDING OF HUMAN PLASMINOGEN AND LACTOFERRIN BY HELICOBACTER-PYLORI COCCOID FORMS

The interactions between Helicobacter pylori spiral and coccoid forms, extracellular matrix (ECM) and plasma proteins were studied in an I-1 25-labelled protein assay, The range of binding of collagen V, plasmin ogen, human lactoferrin (HLf) and vitronectin to coccoid forms of H. p ylori NCTC 11637 was 26-48%. In contrast, binding of radiolabelled fib ronectin and collagen types I and III was low (3-8%), The coccoid form s of 14 strains of H. pylori showed significant HLf binding (median 26 %). With plasminogen, no significant difference was found between bind ing to the coccoid (median = 13%) and spiral (median = 12%) forms, of 13 of the 14 strains of H. pylori tested; the exception was strain NCT C 11637, I-125-plasminogen showed a dose-dependent binding to both the coccoid and spiral forms, Plasminogen binding to both forms was speci fic; the binding was inhibited by non-labelled plasminogen, plasmin, l ysine, EACA (epsilon-aminocaproic acid) but not by fetuin or various c arbohydrates, 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 o f tissue adhesion for various pathogenic bacteria, the coccoid differe ntiated form of H. pylori can be considered as an infective form in th e pathogenesis of helicobacter infection and type B gastritis.