Suppressive effect on polyclonal B-cell activation of a synthetic peptide homologous to a transmembrane component of oncogenic retroviruses.
Purified feline leukemia virus, UV light-inactivated feline leukemia virus, and a synthetic peptide (CKS-17) homologous to a well-conserved region of the transmembrane components of several human and animal retroviruses were each studied for their effects on IgG production by feline peripheral blood lymphocytes. Using a reverse hemolytic plaque assay, both the viable virus and the UV-inactivated feline leukemia virus, but not the CKS-17, activated B lymphocytes to secrete IgG. When staphylococcal protein A, a polyclonal B-cell activator, was used to stimulate IgG synthesis by feline lymphocytes, the viable virus, the UV-inactivated virus, and the CKS-17 peptide each strongly suppressed IgG secretion without compromising viability of the lymphocytes. These findings suggest that the immunosuppressive influences of feline leukemia virus on immunoglobulin synthesis may reside in a conserved portion of the envelope glycoprotein that includes the region homologous to CKS-17.
D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D001402:B-Lymphocytes / Q000276:immunology*; D002415:Cats; D005260:Female; D007074:Immunoglobulin G / Q000032:analysis; D007165:Immunosuppression Therapy; D005256:Leukemia Virus, Feline / Q000276:immunology* / Q000528:radiation effects; D008213:Lymphocyte Activation; D008297:Male; D010455:Peptides / Q000276:immunology*; D014466:Ultraviolet Rays; D014764:Viral Proteins / Q000276:immunology*
D007074:Immunoglobulin G; D010455:Peptides; D014764:Viral Proteins