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Article

Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion.

The Journal of biological chemistry - 9 May 2008

Loch Sandra, Klauschies Florian, Schölz Christian, Verweij Marieke C, Wiertz Emmanuel J H J, Koch Joachim, Tampé Robert

Abstract excerpt

Cytotoxic T lymphocytes eliminate infected cells upon surface display of antigenic peptides on major histocompatibility complex I molecules. To promote immune evasion, UL49.5 of several varicelloviruses interferes with the pathway of major histocompatibility complex I antigen processing. However, the inhibition mechanism has not been elucidated yet. Within the macromolecular peptide-loading complex we identified...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18321854
DOI: 10.1074/jbc.M800226200

Genes

TAP1
TAP2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Signaling of a varicelloviral factor across the endoplasmic reticulum membrane induces destruction of the peptide-loading complex and immune evasion.PMID 18321854Read ↗

The Capacity of UL49.5 Proteins To Inhibit TAP Is Widely Distributed among Members of the Genus VaricellovirusSemantic proximity Read ↗

The herpesvirus UL49.5 protein hijacks a cellular C-degron pathway to drive TAP transporter degradationSemantic proximity Read ↗

Varicellovirus UL49.5 Proteins Differentially Affect the Function of the Transporter Associated with Antigen Processing, TAPSemantic proximity Read ↗

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