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The Journal of Immunology, Vol 155, Issue 6 3092-3101, Copyright © 1995 by American Association of Immunologists

ARTICLES

Differences in the binding of blocking anti-CD11b monoclonal antibodies to the A-domain of CD11b

SM Violette, JR Rusche, SR Purdy, JG Boyd, J Cos and S Silver
Repligen Corporation, Cambridge, MA 02139, USA.

CD11b/CD18 (Mac-1) is a leukocyte integrin that plays a critical role in neutrophil adhesion and the initiation of acute inflammatory responses. Several Mac-1 blocking mAbs bind to the A-domain of CD11b, a approximately 200 amino acid region in the N-terminal portion of the protein that is involved in ligand binding and Mac-1 functional activity. We examined several CD11b blocking mAbs for different patterns of binding to A-domain. We used human/murine chimeric CD11b expression constructs and deletions of the A-domain to examine binding. We describe the binding characteristics of mAbs 60.1, LM2/1, LPM19C, M170, 44, and 904. All of these mAbs, except for 60.1, bind to the C- terminal half of the human A-domain (CD11b181-316). mAb 60.1 was unique in that it required regions of the N- and C-terminal ends of the A- domain for binding. mAbs 60.1, LPM19C, 904, and 44 all required the A- domain to be intact for binding. This suggests that these CD11b mAbs recognize a conformational epitope. LM2/1 was capable of binding to a fragment of the A-domain, CD11b285-300. Inasmuch as this system has been used to define different mAb binding sites, it may be used to analyze specific ligand binding sites in the A-domain of CD11b.


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