Affiliation:
1. Division of Rheumatology and Immunology, Tufts-New England Medical Center, Boston, Massachusetts 02111
Abstract
ABSTRACT
The outer membrane protein p66 of the Lyme disease agent,
Borrelia burgdorferi
, has been identified as a candidate ligand for β
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 α
IIb
β
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 α
IIb
β
3
recognition, suggesting that, as is true for other integrin ligands, the tertiary structure of p66 is important for receptor recognition.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Immunology,Microbiology,Parasitology
Cited by
44 articles.
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