A family of variably expressed outer-membrane proteins (Vomp) mediates adhesion and autoaggregation in Bartonella quintana
| Autor: | Jane E. Koehler, Karen L. Kelminson, Sara Droz, Nicholas W. Lerche, Bruno B Chomel, Peng Zhang, Jeanna S. Goo, Maureen K. Schau, Smitha S. George |
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| Rok vydání: | 2004 |
| Předmět: |
Amino Acid Motifs
Blotting Western Molecular Sequence Data Virulence Biology Virulence factor Bacterial Adhesion Microbiology Bartonella quintana Antigenic variation Animals Humans Trimeric autotransporter adhesin Electrophoresis Gel Two-Dimensional Adhesins Bacterial Conserved Sequence Gene Rearrangement Multidisciplinary Gene rearrangement Biological Sciences biology.organism_classification bacterial infections and mycoses Macaca mulatta Trench Fever Bacterial adhesin Molecular Weight Phenotype Genes Bacterial Models Animal Mutation bacteria Collagen Bacterial outer membrane Bacterial Outer Membrane Proteins Protein Binding |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 101(37) |
| ISSN: | 0027-8424 |
| Popis: | Bartonella species are fastidious, Gram-negative human pathogens that can persist in the host bloodstream for years and bind to and invade several types of host cells. For many pathogens, adhesion to host cells and extracellular matrix (ECM) components is a critical virulence determinant. Bacteria often vary expression of surface adhesins by phase or antigenic variation to subvert the host immune response and permit adaptive interaction with different host structures. We developed a macaque animal model for Bartonella quintana infection to detect changes in bacterial outer-membrane proteins (OMP) during prolonged bloodstream infection. We identified a gene family encoding four highly conserved, 100-kDa, variably expressed OMP (Vomp), two of which function as adhesins. The variable expression of Vomp family members appears to be mediated by deletion of one or more vomp genes during chronic bloodstream infection. vomp deletion was observed also in isolates from humans with chronic B. quintana infection. The Vomp are closely related to the afimbrial adhesin, YadA, a virulence factor of Yersinia enterocolitica . The surface-expressed Vomp contain conserved structural features of YadA, including collagen-binding motifs. We demonstrate that the B. quintana Vomp are multifunctional OMP involved in binding to collagen and autoaggregation: VompC confers the ability to bind collagen IV, and VompA is necessary and sufficient for autoaggregation. The B. quintana Vomp are members of the newly recognized family of YadA-like trimeric autotransporters; the Vomp constitute a multigene family, they are variably expressed, and different virulence properties are attributable to individual Vomp family members. |
| Databáze: | OpenAIRE |
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