Published November 1995
| Version public
Journal Article
The MHC class I homolog encoded by human cytomegalovirus binds endogenous peptides
Creators
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1.
California Institute of Technology
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2.
Harvard University
Abstract
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 1 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.
Additional Information
© 1995 Cell Press. Received 19 July 1995, Revised 7 September 1995. We thank D. Spector for the DNA encoding UL 18; A. Chirino for help with Figure 1; T. Chapman for providing purified UL 18 and for many helpful discussions; R. Robinson, E. Spooner, and V. Bailey for expertise in HPLC, mass spectrometry, and sequencing; the Caltech microchemical facility and colleagues in the Bjorkman lab for critical reading of the manuscript. This work was supported by the Howard Hughes Medical Institute (M.L.F., J.L.J., P.J.B.) and the Arthritis Foundation (P.J.B.).Additional details
Identifiers
- Eprint ID
- 75752
- Resolver ID
- CaltechAUTHORS:20170405-152523311
Funding
- Howard Hughes Medical Institute (HHMI)
Dates
- Created
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2017-04-05Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field