title: The Chlamydia outer membrane protein OmcB is required for adhesion and exhibits biovar-specific differences in glycosaminoglycan binding.
abstract: Chlamydia pneumoniae, an obligate intracellular human pathogen, causes a number of respiratory diseases. We explored the role of the conserved OmcB protein in C. pneumoniae infections, using yeast display technology. (i) Yeast cells presenting OmcB were found to adhere to human epithelial cells. (ii) Pre-incubation of OmcB yeast cells with heparin, but not other glycosaminoglycans (GAGs), abrogated adhesion. (iii) Pre-treatment of the target cells with heparinase inhibited adherence, and GAG-deficient CHO cell lines failed to bind OmcB yeast. (iv) A heparin-binding motif present near the N-terminus of OmcB is required for host cell binding. (v) Pre-treatment of chlamydial elementary bodies (EBs) with anti-OmcB antibody or pre-incubation of target cells with recombinant OmcB protein reduced infectivity upon challenge with C. pneumoniae. (vi) Adhesion of fluorescently labelled EBs to epithelial or endothelial cells was abrogated by prior addition of heparin or OmcB protein. Thus, C. pneumoniae OmcB is an adhesin that binds heparan sulphate-like GAGs. OmcB from Chlamydia trachomatis serovar L1 also adheres to human cells in a heparin-dependent way, unlike its counterpart from serovar E. We show that a single position in the OmcB sequence determines heparin dependence/independence, and variations there may reflect differences between the two serovars in cell tropism and disease pattern.
authors: Lehrstuhl für Funktionelle Genomforschung der Mikroorganismen, Heinrich-Heine-Universität, 40225 Düsseldorf, Germany.
authors: Katja
authors: K
authors: Moelleken
authors: Johannes H
authors: JH
authors: Hegemann
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001422:Bacterial Adhesion; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D016466:CHO Cells; D002460:Cell Line; D002690:Chlamydia Infections / Q000382:microbiology; D002692:Chlamydia trachomatis / Q000145:classification / Q000472:pathogenicity; D016993:Chlamydophila pneumoniae / Q000472:pathogenicity / Q000502:physiology*; D006224:Cricetinae; D003412:Cricetulus; D006025:Glycosaminoglycans / Q000378:metabolism*; D006497:Heparan Sulfate / Q000378:metabolism; D054884:Host-Pathogen Interactions; D006801:Humans; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000502:physiology; D012703:Serotyping
chemical_list: D001425:Bacterial Outer Membrane Proteins; D006025:Glycosaminoglycans; D006497:Heparan Sulfate; D011993:Recombinant Fusion Proteins; C436968:OmcB protein, bacteria