ArticleJournal of virology2014
Human herpesvirus 7 U21 tetramerizes to associate with class I major histocompatibility complex molecules.
Article in Journal of virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Viral manipulation of the HLA class I antigen processing and presentation pathway.Frontiers in immunology · 2025Review
- Characterization of the HHV-6B U20 Immunoevasin.Journal of virology · 2023Article
- Structural Models for Roseolovirus U20 And U21: Non-Classical MHC-I Like Proteins From HHV-6A, HHV-6B, and HHV-7.Frontiers in immunology · 2022Review
- Evasion of the Host Immune Response by Betaherpesviruses.International journal of molecular sciences · 2021Review
- The Roseoloviruses Downregulate the Protein Tyrosine Phosphatase PTPRC (CD45).Journal of virology · 2021Article
- Article
- Analytical ultracentrifuge: an ideal tool for characterization of non-coding RNAs.European biophysics journal : EBJ · 2020Review
- HHV-7 U21 exploits Golgi quality control carriers to reroute class I MHC molecules to lysosomes.Molecular biology of the cell · 2020Article
- Advances in the Characterization of the T-Cell Response to Human Herpesvirus-6.Frontiers in immunology · 2018Review
- Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT.Acta crystallographica. Section D, Biological crystallography · 2015Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
unlabelledThe U21 gene product from human herpesvirus 7 binds to and redirects class I major histocompatibility complex (MHC) molecules to a lysosomal compartment. The molecular mechanism by which U21 reroutes class I MHC molecules to lysosomes is not known. Here, we have reconstituted the interaction between purified soluble U21 and class I MHC molecules, suggesting that U21 does not require additional cellular proteins to interact with class I MHC molecules. Our results demonstrate that U21, itself predicted to contain an MHC class I-like protein fold, interacts tightly with class I MHC molecules as a tetramer, in a 4:2 stoichiometry. These observations have helped to elucidate a refined model describing the mechanism by which U21 escorts class I MHC molecules to the lysosomal compartment. IMPORTANCE: In this report, we show that the human herpesvirus 7 (HHV-7) immunoevasin U21, itself a class I MHC-like protein, binds with high affinity to class I MHC molecules as a tetramer and escorts them to lysosomes, where they are degraded. While many class I MHC-like molecules have been described in detail, this unusual viral class I-like protein functions as a tetramer, associating with class I MHC molecules in a 4:2 ratio, illuminating a functional significance of homooligomerization of a class I MHC-like protein.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.