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- W2068259161 abstract "The spirochaetal agents of Lyme disease, Borrelia burgdorferi (sensu lato) bind to integrins αIIbβ3, αvβ3 and α5β1 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 β3-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 β3-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 αvβ3, but not to the parental cell line, which expresses no β3-chain integrins. Localization of p66 on the surface of B. burgdorferi, the ability of recombinant forms of the protein to bind to β3-chain integrins and the fact that p66 and B. burgdorferi bind to β3-chain integrins in a mutually exclusive manner make p66 an attractive candidate bacterial ligand for integrins αIIbβ3 and αvβ3." @default.
- W2068259161 created "2016-06-24" @default.
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- W2068259161 date "1999-12-01" @default.
- W2068259161 modified "2023-10-01" @default.
- W2068259161 title "Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library" @default.
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- W2068259161 doi "https://doi.org/10.1046/j.1365-2958.1999.01654.x" @default.
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