IDENTIFICATION OF NATURAL RESISTANCE-ASSOCIATED MACROPHAGE PROTEIN INPERIPHERAL-BLOOD LYMPHOCYTES

Natural resistance-associated macrophage protein gene (Nramp) was isol ated from the gene locus Lsh/Ity/Bcg, which regulates macrophage activ ation for antimicrobial activity against intracellular pathogens. The deduced protein sequence encodes an integral membrane protein that has structural homology with known prokaryotic and eukaryotic transport s ystems. In the present study, a polyclonal antibody was raised with th e synthetic peptide of the carboxy-terminal 17 amino acids of human Nr amp. The protein product of the gene is apparently present in human pe ripheral blood lymphocyte (PBL) as a 60 MD a protein recognized by the antibody, which is consistent with the calculated molecular mass. Bac terial lipopolysaccharide or interferon-gamma did not appear to stimul ate the level of Nramp expression in PBL.