Delineation of Borrelia burgdorferi p66 sequences required for integrin alpha(IIb)beta(3) recognition.
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.
Defoe
G
G
Division of Rheumatology and Immunology, Tufts-New England Medical Center, Boston, Massachusetts 02111, USA.
Coburn
J
J
D001422:Bacterial Adhesion; D001426:Bacterial Proteins; D015748:Borrelia burgdorferi Group / Q000502:physiology*; D004492:Edetic Acid / Q000494:pharmacology; D010446:Peptide Fragments / Q000378:metabolism; D010456:Peptides, Cyclic / Q000494:pharmacology; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000378:metabolism*; D018272:Porins / Q000737:chemistry / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism
D001426:Bacterial Proteins; C107893:Oms66 protein, Borrelia; D010446:Peptide Fragments; D010456:Peptides, Cyclic; D019039:Platelet Glycoprotein GPIIb-IIIa Complex; D018272:Porins; D011994:Recombinant Proteins; C119707:cyclo(S,S)KYGCRGDWPC; D004492:Edetic Acid