Abstract
Primary infection with human cytomegalovirus (HCMV) is persistent and widespread, with symptoms that are mostly subclinical but can cause serious illness or death, particularly in immunosuppressed patients1,2. Recently3, proteins from HCMV were shown to bind β2-microglobulin (β2-m) a protein that is normally found associated with the class-I major histocompatibility complex (MHC) antigens, which are essential for self-non-self recognition in the immune response4. These findings led to the proposal that the virus may use β2-m binding as an infection mechanism5. Here we present evidence from DNA sequence analysis that HCMV encodes a molecule similar to the MHC class-I antigens of higher eucaryotes, and propose that this protein is responsible for the observed β2-m binding. The deduced amino-acid sequence of the HCMV class-I-like protein reveals conservation of typical features of class-I structure, but we predict that the gene is not spliced, in contrast to the cellular genes.
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Beck, S., Barrell, B. Human cytomegalovirus encodes a glycoprotein homologous to MHC class-I antigens. Nature 331, 269–272 (1988). https://doi.org/10.1038/331269a0
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DOI: https://doi.org/10.1038/331269a0
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