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Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I.

Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Research Abstract Details 

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  • Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Abstract Text:

    christopher t cornellChristopher T Cornell,william b kiossesWilliam B Kiosses,stephanie harkinsStephanie Harkins,j lindsay whittonJ Lindsay Whitton,

    Picornaviruses carry a small number of proteins with diverse functions that subvert and exploit the host cell. We have previously shown that three coxsackievirus B3 (CVB3) proteins (2B, 2BC, and 3A) target the Golgi complex and inhibit protein transit. Here we investigate these effects in more detail and evaluate the distribution of major histocompatibility complex (MHC) class I molecules, which are critical mediators of the CD8(+) T-cell response. We report that concomitant with viral protein synthesis, MHC class I surface expression is rapidly downregulated during infection. However, this phenomenon may not result solely from inhibition of anterograde trafficking; we propose a new mechanism whereby the CVB3 2B and 2BC proteins upregulate the internalization of MHC class I (and possibly other surface proteins), perhaps by focusing of endocytic vesicles at the Golgi complex. Thus, our findings indicate that CVB3 carries at least three nonstructural proteins that directionally complement one another; 3A disrupts the Golgi complex to inhibit anterograde transport, while 2B and/or 2BC upregulates endocytosis, rapidly removing proteins from the cell surface. Taken together, these effects may render CVB3-infected cells invisible to CD8(+) T cells and untouchable by many antiviral effector molecules. This has important implications for immune evasion by CVB3.

    Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Publishing Authors By Initials

    ct cornellCT Cornell,wb kiossesWB Kiosses,s harkinsS Harkins,jl whittonJL Whitton,

    For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

    PUBMED ID PMID:

    MEDLINE DATE:

    Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of virology

    VOLUME: 81

    Page Numbers: 6785-97

    Journal Abbreviation: J. Virol.

    ISSN: 0022-538X

    DAY: 18

    MONTH: 04

    YEAR: 2007

    Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 113724

    Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Keywords Mesh Terms:

    KEYWORDS: Viral Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I. Information

    Substance Name: coxsackie B3 virus protein 2B

    Registry Number: 0

    Grant and Affiliation Information for Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I.

    AFFILIATION: Molecular and Integrative Neurosciences Department, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: R01 AI-42314

    ACRONYM: AI

    MEDLINETA: J Virol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

    Coxsackievirus B3 proteins directionally complement each other to downregulate surface major histocompatibility complex class I Related Publications

     

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