Monoclonal Antibodies Against Human LFA-1 Cross-React with Porcine LFA-1 and Inhibit Porcine T-Lymphocyte and Natural Killer Cell Function
Abstract
We have tested five monoclonal antibodies against polypeptides of the human LFA-1/Mac-1/p150-95 glycoprotein family for cross-reactivity with procine leukocytes. Three monoclonal antibodies against the shared beta-subunit were found to react with porcine antigens. One anti-beta-subunit monoclonal antibody precipitated the porcine polypeptides corresponding to the alpha and beta subunits of LFA-1 and a polypeptide corresponding to the p150 alpha-chain seen on human macrophages and granulocytes. Results of two-dimensional electrophoretic studies suggested that the porcine p150 alpha-subunit is much more highly acidic than the human equivalent. Two anti-beta-subunit antibodies precipitated only the subunits of LFA-1. Monoclonal antibodies recognizing the human LFA-1 and Mac-1 alpha-subunits did not react with pig cells. The anti- beta-subunit antibodies inhibited mitogenic and allogeneic stimulation of procine lymphocytes as well as cytotoxic T cell and natural killer cell-mediated lysis of target cells. Inhibition of cytotoxic T cell function by an anti-beta- subunit antibody was found to be additive with blockade by an antibody against the procine CD8 antigen. The results show that porcine leukocytes express the LFA-1 molecule and that porcine LFA-1 is involved in T cell and NK cell functions as previously shown in human and murine studies. Keywords: Lymphocyte function associated antigens, Allografts, Graft versus host disease, Immunology, Preventive medicine, Transplantation.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1986
- Accession Number
- ADA198954
Entities
People
- J. T. August
- James E. Hildreth
- Mark D. Pescovitz
- Valerie Holt
Organizations
- Johns Hopkins University