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Delineation of Borrelia burgdorferi p66 sequences required for integrin alpha(IIb)beta(3) recognition. Infect Immun 2001 May;69(5):3455-9 PMID: 11292775 PMCID: PMC98311

Pubmed ID



The outer membrane protein p66 of the Lyme disease agent, Borrelia burgdorferi, has been identified as a candidate ligand for beta(3)-chain integrins. To identify portions of p66 required for integrin recognition, fusions of maltose-binding protein to fragments of p66 were tested for binding to integrin alpha(IIb)beta(3), and synthetic peptides derived from the p66 amino acid sequence were tested for the ability to inhibit B. burgdorferi attachment to the same integrin. The data identify two noncontiguous segments of p66 that are important for alpha(IIb)beta(3) recognition, suggesting that, as is true for other integrin ligands, the tertiary structure of p66 is important for receptor recognition.

Author List

Defoe G, Coburn J


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


2-s2.0-0035055365   39 Citations

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

Bacterial Adhesion
Bacterial Proteins
Borrelia burgdorferi Group
Edetic Acid
Peptide Fragments
Peptides, Cyclic
Platelet Glycoprotein GPIIb-IIIa Complex
Recombinant Proteins
jenkins-FCD Prod-332 f92a19b0ec5e8e1eff783fac390ec127e367c2b5