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Targeted mutation of the outer membrane protein P66 disrupts attachment of the Lyme disease agent, Borrelia burgdorferi, to integrin alphavbeta3. Proc Natl Acad Sci U S A 2003 Jun 10;100(12):7301-6 PMID: 12748384 PMCID: PMC165870

Pubmed ID

12748384

Abstract

Borrelia burgdorferi, the agent of Lyme disease, expresses several adhesion molecules that are probably required for initial establishment of infection in mammalian hosts, and for colonization of various tissues within the host. The B. burgdorferi outer membrane protein P66 was previously identified as a ligand for beta3-chain integrins by using a variety of biochemical approaches. Although the earlier data suggested that P66 is an adhesin that mediates B. burgdorferi attachment to beta3-chain integrins, lack of genetic systems in B. burgdorferi precluded definitive demonstration of a role for P66 in beta3 integrin attachment by intact borreliae. Recent advances in the genetic manipulation of B. burgdorferi have now made possible the targeted disruption of the p66 gene. Mutants in p66 show dramatically reduced attachment to integrin alphavbeta3. This is, to our knowledge, the first description of the targeted disruption of a candidate B. burgdorferi virulence factor with a known biochemical function that can be quantified, and demonstrates the importance of B. burgdorferi P66 in the attachment of this pathogenic spirochete to a human cell-surface receptor.

Author List

Coburn J, Cugini C

Author

Jenifer Coburn PhD Professor in the Medicine department at Medical College of Wisconsin




Scopus

2-s2.0-0038809086   72 Citations

MESH terms used to index this publication - Major topics in bold

Bacterial Adhesion
Bacterial Proteins
Binding Sites
Borrelia burgdorferi
Genes, Bacterial
Humans
In Vitro Techniques
Integrin alphaVbeta3
Lyme Disease
Mutation
Porins
jenkins-FCD Prod-299 9ef562391eceb2b8f95265c767fbba1ce5a52fd6