The immunology of companion animals: reagents and therapeutic strategies with potential veterinary and human clinical applications

Cobbold, Stephen; Holmes, Mark A.; Willett, Brian J.

doi:10.1016/0167-5699(94)90171-6

Cited by 22 publications

(2 citation statements)

References 15 publications

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“…The data on tissue distribution and the N-terminal sequence provide strong evidence that mAb 3/22 recognizes the rabbit homologue of the CDllc integrin a chain. We have found no evidence for a fourth C D l l a chain as has been reported for the dog [42][43][44]. The N-terminal sequence of rabbit CDllc shows it to be homologous with both human CDllc and rabbit CDllb.…”

Section: Discussioncontrasting

confidence: 51%

A monoclonal antibody, 3/22, to rabbit CD11c which induces homotypic T cell aggregation: evidence that ICAM‐1 is a ligand for CD11c/CD18

Blackford

Reid

Pappin³

et al. 1996

Eur J Immunol

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The rabbit CD11c molecule has been characterized by use of new monoclonal antibody, mAb 3/22. Expression of the p150,95 integrin (CD11c/CD18) has been shown by flow cytometry and immunohistochemistry to be restricted to monocytes, macrophages, dendritic cells and a small population of lymphocytes in peripheral blood. No expression on neutrophils could be demonstrated. Incubation of the newly derived CD8+ T cell line, BJ/873, with mAb 3/22 causes homotypic aggregation, which has been shown to be cell surface event that is not dependent on intracellular signaling or on receptor cross-linking. Inhibition studies show that the ligands responsible for this aggregation are CD11c/CD18 and ICAM-1, both of which are expressed on BJ/873. One other rabbit T cell line, K34, that also expresses p150,95 and ICAM-1, shows a similar aggregation response when stimulated with 3/22. Cell lines that express p150,95 but not ICAM-1 do not aggregate. These observations suggest that ICAM-1 is a ligand for activated p150,95.

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Section: Discussioncontrasting

confidence: 51%

A monoclonal antibody, 3/22, to rabbit CD11c which induces homotypic T cell aggregation: evidence that ICAM‐1 is a ligand for CD11c/CD18

Blackford

Reid

Pappin³

et al. 1996

Eur J Immunol

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“…Activated CR3 plays an essential role in immune clearance by facilitating neutrophil adhesion to endothelium, transendothelial migration, and phagocytosis of serum-opsonized particles (reviewed in reference 5). CR3 is one of the four members comprising the/32 integrin subfamily that share a common /3 subunit (CD18), but have distinct (CDll) subunits, the other three members being LFA-1 (CDlla/CD18, otL/~2, TA-1), p150,95 (CDllc/CD18, t~X/~2, Leu-M5), and the recently described macrophage-restricted CDlld/CD18 (otTM/32) (17) (reviewed in reference 4). CR3 binds in a divalent cation-dependent manner to several ligands including iC3b, the major complement opsonin (9,10,60), fibrinogen (1), and CD54 (ICAM-1) (21), through non-Arg-Gly-Asp-containing sequences (2,53,55).…”

mentioning

confidence: 99%

The A-domain of beta 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF.

Rieu

Ueda

Haruta

et al. 1994

The Journal of Cell Biology

106

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Abstract. The A-domain is a ,,o200-amino acid peptide present within structurally diverse proadhesive proteins including seven integrins. A recombinant form of the A-domain of/32 integrins CR3 and LFA-1 has been recently shown to bind divalent cations and to contain binding sites for protein ligands that play essential roles in leukocyte trafficking to inflammatory sites, phagocytosis and target cell killing. In this report we demonstrate that the neutrophil adhesion inhibitor, NIF produced by the hookworm Ancylostoma caninum is a selective CDllb A-domain binding protein. NIF bound directly, specifically and with high affinity (Kd of ~1 nM) to recombinant CD1 lb A-domain (rllbA). The binding reaction was characterized by rapid association and very slow dissociation, and was blocked by an anti-rllbA monoclonal antibody. No binding was observed to rCDllaA. The NIF-rllbA interaction required divalent cations, and was absent when the mutant rllbA D140GS/AGA (that lacks divalent cation binding capacity) was used. The NIF binding site in rllbA was mapped to four short peptides, one of which being an iC3b binding site. The interaction of NIF with CR3 in intact cells followed similar binding kinetics to those with rllbA, and occurred with similar affinity in resting and activated human neutrophils, suggesting that the NIF epitope is activation independent. Binding of NIF to CR3 blocked its ability to bind to its ligands iC3b, fibrinogen, and CD54, and inhibited the ability of human neutrophils to ingest serum opsonized particles. NIF thus represents the first example of a disintegrin that targets the integrin A-domain, and is likely to be used by the hookworm to evade the host's inflammatory response. The unique structure of NIF, which lacks a disintegrin motif, emphasizes basic structural differences in antagonists targeting A + and A-integrins, that should be valuable in drug design efforts aimed at generating novel therapeutics. Identification of the region in NIF mediating A-domain binding should also be useful in this regard, and may, as in the case of disintegrins, unravel a new structural motif with cellular counterparts mediating important physiologic functions.

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Cluster of Differentiation (CD) Antigens

Wilkerson¹,

Springer²

2022

Schalm's Veterinary Hematology

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The immunology of companion animals: reagents and therapeutic strategies with potential veterinary and human clinical applications

Cited by 22 publications

References 15 publications

A monoclonal antibody, 3/22, to rabbit CD11c which induces homotypic T cell aggregation: evidence that ICAM‐1 is a ligand for CD11c/CD18

A monoclonal antibody, 3/22, to rabbit CD11c which induces homotypic T cell aggregation: evidence that ICAM‐1 is a ligand for CD11c/CD18

The A-domain of beta 2 integrin CR3 (CD11b/CD18) is a receptor for the hookworm-derived neutrophil adhesion inhibitor NIF.

Cluster of Differentiation (CD) Antigens

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