Human major histocompatibility complex class I antigens: Residues 61-83 of the HLA-B7 heavy chain specify an alloreactive site
Article
Walker, LE, Ketler, TA, Houghten, RA et al. (1985). Human major histocompatibility complex class I antigens: Residues 61-83 of the HLA-B7 heavy chain specify an alloreactive site
. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 82(2), 539-542. 10.1073/pnas.82.2.539
Walker, LE, Ketler, TA, Houghten, RA et al. (1985). Human major histocompatibility complex class I antigens: Residues 61-83 of the HLA-B7 heavy chain specify an alloreactive site
. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 82(2), 539-542. 10.1073/pnas.82.2.539
A chemically synthesized peptide (Asp-Arg-Asn-Thr-Gln-Ile-Tyr-Lys-Ala-Gln-Ala-Gln-Thr-Asp-Arg-Glu-Ser-Leu- Arg-Asn-Leu-Arg-Gly), homologous to residues 61-83 of the HLA-B7 heavy chain, induced antibodies that specifically recognized the HLA heavy chain-β2-microglobulin complex and the free heavy chain of the HLA-B7 antigen. These antibodies specifically immunoprecipitated the HLA-B7 β2-microglobulin complex solubilized from human lymphoblastoid cells by nonionic detergents and reacted with free HLA-B7 heavy chains in blots on nitrocellulose. These observations suggest that the antigenic conformation of this region of the HLA-B7 molecule is independent of the presence of β2-microglobulin and that amino acid residues 61-83 mimic an alloreactive site expressed by the HLA-B7 antigen.
