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Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library. Mol Microbiol 1999 Dec;34(5):926-40 PMID: 10594819

Pubmed ID



The spirochaetal agents of Lyme disease, Borrelia burgdorferi (sensu lato) bind to integrins alphaIIbbeta3, alphavbeta3 and alpha5beta1 in purified form and on the surfaces of human cells. Using a phage display library of B. burgdorferi (sensu stricto) DNA, a candidate ligand for beta3-chain integrins was identified. The native B. burgdorferi protein, termed p66, is known to be recognized by human Lyme disease patient sera and to be expressed on the surface of the spirochaete. We show here that recombinant p66 binds specifically to beta3-chain integrins and inhibits attachment of intact B. burgdorferi to the same integrins. When expressed on the surface of Escherichia coli, this protein increases the attachment of E. coli to a transfected cell line that expresses alphavbeta3, but not to the parental cell line, which expresses no beta3-chain integrins. Localization of p66 on the surface of B. burgdorferi, the ability of recombinant forms of the protein to bind to beta3-chain integrins and the fact that p66 and B. burgdorferi bind to beta3-chain integrins in a mutually exclusive manner make p66 an attractive candidate bacterial ligand for integrins alphaIIbbeta3 and alphavbeta3.

Author List

Coburn J, Chege W, Magoun L, Bodary SC, Leong JM


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


2-s2.0-0033233457   92 Citations

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

ATP-Binding Cassette Transporters
Antigens, CD
Bacterial Adhesion
Bacterial Proteins
Borrelia burgdorferi Group
Carrier Proteins
Cell Line
Escherichia coli
Escherichia coli Proteins
Integrin beta3
Maltose-Binding Proteins
Monosaccharide Transport Proteins
Peptide Library
Platelet Membrane Glycoproteins
Recombinant Fusion Proteins
jenkins-FCD Prod-332 f92a19b0ec5e8e1eff783fac390ec127e367c2b5