Monoclonal antibody 2F4/11 recognizes the α chain of a porcine β2 integrin involved in adhesion and complement mediated phagocytosis

The characterization of a new mAb, named 2F4/11, specific for porcine myelomonocytic cells is described. This mAb immunoprecipitates a non-covalently linked heterodimer of 155,000/95,000, which is expressed by granulocytes, monocytes and tissue macrophages but not by lymphocytes, erythrocytes or platelets. Immunoblot analysis localizes the 2F4/11 epitope on the largest subunit of the heterodimer. Mab 2F4/11 is able to block phagocytosis of complement-oppsonized zymosan particles by PMN granulocytes and alveolar macrophages, as well as adherence to plastic surfaces of PMA-activated PMN. Together, these results suggest that mAb 2F4/11 recognizes the CD11b or α chain of the porcine complement type 3 receptor (CR3).

Bibliographic Details

Main Authors:	Bullido, R., Alonso, F., Gómez del Moral, M., Ezquerra Martínez, Ángel, Alvarez, B., Ortuño, E., Domínguez, J.
Format:	artículo biblioteca
Language:	English
Published:	Elsevier 1996
Subjects:	Monoclonal antibody, Granulocyte, Monocyte, Macrophage, CD1 lb, Mac-i, Integrin: (Pig),
Online Access:	http://hdl.handle.net/20.500.12792/4874 http://hdl.handle.net/10261/289880
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