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. 1990 Jun;58(6):1749–1756. doi: 10.1128/iai.58.6.1749-1756.1990

Identification of Campylobacter jejuni surface proteins that bind to Eucaryotic cells in vitro.

M A de Melo 1, J C Pechère 1
PMCID: PMC258718  PMID: 2160431

Abstract

To understand the role of Campylobacter jejuni surface proteins in the interaction of C. jejuni with cultured mammalian cell lines in vitro, we developed a ligand-binding assay. This procedure allowed us to antigenically identify C. jejuni outer membrane proteins (OMPs) that attach to intact host cell membranes. OMPs isolated from an invasive strain and a less invasive strain were antigenically indistinguishable. However, we found that proteins with molecular masses of 28 and 32 kilodaltons (kDa) from just the invasive strain bound to HEp-2 cell monolayers. Binding of the 32-kDa OMP was cell line specific and correlated directly with the ability of the invasive C. jejuni strain to penetrate. Such a correlation was probably also true for the 28-kDa OMP. We also investigated the binding of glycine acid extracts with cell line HEp-2. We identified four proteins with apparent molecular masses of 28, 32, 36, and 42 kDa in the invasive strain extracts that bound to HEp-2 cells. In contrast, only the 36-kDa protein from the less invasive strain bound to HEp-2 cells. Our data suggest that binding of these surface exposed proteins may play a key role in C. jejuni-host cell interactions and ultimate invasion.

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