The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides.
The ability of a human cytomegalovirus-encoded homolog of MHC class I molecules to serve as a peptide receptor was investigated. Sequencing of peptide material eluted from the purified viral protein revealed a mixture of endogenous peptides with characteristics similar to those eluted from conventional class I molecules, that is, anchor residues, and a predominance of short peptides derived from cytoplasmic proteins. The possible function(s) of this viral MHC homolog are discussed in light of the finding that it binds endogenous peptides.
Fahnestock
M L
ML
Division of Biology, California Institute of Technology, Pasadena 91125, USA.
Johnson
J L
JL
Feldman
R M
RM
Neveu
J M
JM
Lane
W S
WS
Bjorkman
P J
PJ
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002478:Cells, Cultured; D006224:Cricetinae; D003587:Cytomegalovirus / Q000737:chemistry*; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000502:physiology*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding / Q000502:physiology; D014162:Transfection; D014764:Viral Proteins / Q000737:chemistry* / Q000502:physiology*
D015395:Histocompatibility Antigens Class I; D014764:Viral Proteins