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Journal of virology2012; 86(7); 3554-3563; doi: 10.1128/JVI.06994-11

Identification and characterization of equine herpesvirus type 1 pUL56 and its role in virus-induced downregulation of major histocompatibility complex class I.

Abstract: Major histocompatibility complex class I (MHC-I) molecules play an important role in host immunity to infection by presenting antigenic peptides to cytotoxic T lymphocytes (CTLs), which recognize and destroy virus-infected cells. Members of the Herpesviridae have developed multiple mechanisms to avoid CTL recognition by virtue of downregulation of MHC-I on the cell surface. We report here on an immunomodulatory protein involved in this process, pUL56, which is encoded by ORF1 of equine herpesvirus type 1 (EHV-1), an alphaherpesvirus. We show that EHV-1 pUL56 is a phosphorylated early protein which is expressed as different forms and predominantly localizes to Golgi membranes. In addition, the transmembrane (TM) domain of the type II membrane protein was shown to be indispensable for correct subcellular localization and a proper function. pUL56 by itself is not functional with respect to interference with MHC-I and likely needs another unidentified viral protein(s) to perform this action. Surprisingly, pUL49.5, an inhibitor of the transporter associated with antigen processing (TAP) and encoded by EHV-1 and related viruses, appeared not to be required for pUL56-induced early MHC-I downmodulation in infected cells. In conclusion, our data identify a new immunomodulatory protein, pUL56, involved in MHC-I downregulation which is unable to perform its function outside the context of viral infection.
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Publication Date: 2012-01-25 PubMed ID: 22278226PubMed Central: PMC3302497DOI: 10.1128/JVI.06994-11Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research focuses on unraveling the role of a protein called pUL56 of the equine herpesvirus type 1 (EHV-1) in suppressing the host’s immune response. The study shows that pUL56 may have a part in reducing the expression of major histocompatibility complex class I (MHC-I) molecules, which are crucial to the host’s immune defense against viral infections.

Characterization of pUL56 Protein

  • The researchers identified that pUL56 is produced early in the viral infection process and modifies itself through a process called phosphorylation.
  • The protein is presented in various forms and mostly associates with the Golgi membranes, a part of the cell involved in packaging proteins for transport.
  • The transmembrane domain, a part of the protein that crosses through the cell membrane, is crucial for the protein’s proper functioning and localization within the cell.

pUL56 Role in MHC-I Downregulation

  • pUL56 potentially plays a role in reducing the expression of MHC-I on the cell surface, a mechanism that helps the virus evade detection by the host’s immune system.
  • However, pUL56 cannot interfere with MHC-I on its own and likely requires other yet unidentified viral proteins to execute its action.

Surprising Findings and Conclusions

  • The study reveals that another viral protein, pUL49.5, which is known to inhibit the antigen-processing mechanism, doesn’t seem to be necessary for the early downregulation of MHC-I triggered by pUL56. This indicates that the two proteins likely operate through different mechanisms.
  • The researchers concluded by identifying pUL56 as a new protein involved in immunomodulation. However, it appears to be functional only within the context of a viral infection and cannot exhibit its function independently.

Cite This Article

APA
Ma G, Feineis S, Osterrieder N, Van de Walle GR. (2012). Identification and characterization of equine herpesvirus type 1 pUL56 and its role in virus-induced downregulation of major histocompatibility complex class I. J Virol, 86(7), 3554-3563. https://doi.org/10.1128/JVI.06994-11

Publication

Journal of virology
ISSN: 1098-5514
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 86
Issue: 7
Pages: 3554-3563

Researcher Affiliations

Ma, Guanggang
  • Institut für Virologie, Freie Universität Berlin, Berlin, Germany. no.34@fu-berlin.de
Feineis, Silke
    Osterrieder, Nikolaus
      Van de Walle, Gerlinde R

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Base Sequence
        • Cell Line
        • Down-Regulation
        • Gene Expression Regulation, Viral
        • Herpesviridae Infections / genetics
        • Herpesviridae Infections / immunology
        • Herpesviridae Infections / veterinary
        • Herpesvirus 1, Equid / genetics
        • Herpesvirus 1, Equid / immunology
        • Histocompatibility Antigens Class I / genetics
        • Histocompatibility Antigens Class I / immunology
        • Horse Diseases / genetics
        • Horse Diseases / immunology
        • Horses
        • Humans
        • Molecular Sequence Data
        • Viral Proteins / genetics
        • Viral Proteins / immunology

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