Monoclonal antibody 2F4/11 recognizes the alpha chain of a porcine beta 2 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-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).
Bullido
R
R
Centro de Investigación en Sanidad Animal, INIA, Valdeolmos, Madrid, Spain.
Alonso
F
F
Gómez del Moral
M
M
Ezquerra
A
A
Alvarez
B
B
Ortuño
Domínguez
J
J
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D018821:CD18 Antigens / Q000276:immunology*; D002448:Cell Adhesion / Q000276:immunology; D003167:Complement Activation; D009000:Monocytes / Q000166:cytology / Q000276:immunology*; D009928:Organ Specificity; D010587:Phagocytosis / Q000276:immunology; D013552:Swine
D000911:Antibodies, Monoclonal; D018821:CD18 Antigens