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

descriptionPublicationkeyboard_double_arrow_right Article 01 Jan 1996 Spain English Publisher:Elsevier BVJournal:Journal of immunological methods, volume 195 (issn: 0022-1759,

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Authors: Bullido, R.; Alonso, Fernando; Gómez del Moral, M.; Ezquerra Martínez, Ángel; Álvarez, Belén; Ortuño, E.; Domínguez, Javier;

pmid: 8814327

handle: 10261/289880

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

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Abstract

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-opsonized 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 alpha chain of the porcine complement type 3 receptor (CR3).

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Spain

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Keywords

Monoclonal antibody, Integrin: (Pig), Macrophage, Swine, Antibodies, Monoclonal, Granulocyte, Monocyte, CD1 lb, Monocytes, Phagocytosis, Organ Specificity, CD18 Antigens, Cell Adhesion, Animals, Mac-i, Complement Activation

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