Beta 2 (CD18) mutations abolish ligand recognition by I domain integrins LFA-1 (alpha L beta 2, CD11a/CD18) and MAC-1 (alpha M beta 2, CD11b/CD18) - PubMed (original) (raw)
. 1995 Jan 6;270(1):94-8.
doi: 10.1074/jbc.270.1.94.
Affiliations
- PMID: 7814426
- DOI: 10.1074/jbc.270.1.94
Free article
Beta 2 (CD18) mutations abolish ligand recognition by I domain integrins LFA-1 (alpha L beta 2, CD11a/CD18) and MAC-1 (alpha M beta 2, CD11b/CD18)
M L Bajt et al. J Biol Chem. 1995.
Free article
Abstract
The "I" domains of the beta 2 (CD18) leukocyte integrins are implicated in ligand binding function. Moreover, rather than recognizing linear peptide sequences, this class of integrins generally recognizes multiple discontinuous sites on immunoglobulin superfamily adhesion receptors. A conserved cluster of oxygenated residues is involved in ligand recognition by beta 1 and beta 3 integrins. In the present study, we evaluated the role of this region in the I domain-containing beta 2 integrins. Recombinant alpha L beta 2 (LFA-1, CD11a/CD18) and alpha M beta 2 (MAC-1, CD11b/CD18) were expressed on COS cells, and function was assessed by adhesion to ICAM-1 or iC3b, respectively. Alanine substitution at position Asp134 or Ser136 in beta 2 produced a complete loss in the capacity of both alpha L beta 2 and alpha M beta 2 to support cell adhesion. In contrast, substitution at Asp128 or Ser138 resulted in loss of beta 2 surface expression when co-transfected with alpha L (CD11a) or alpha M (CD11b). These data provide the first evidence for involvement of the beta 2 subunit in ligand binding to I domain integrins.
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