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J Cell Sci. 2016 Jan 1;129(1):219-27. doi: 10.1242/jcs.175620. Epub 2015 Nov 2.

The murine cytomegalovirus immunoevasin gp40 binds MHC class I molecules to retain them in the early secretory pathway.

Author information

1
Department of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany.
2
Institute of Biology, Center for Structural and Cell Biology in Medicine, University of Lübeck, 23562 Lübeck, Germany.
3
Institute of Virology, University Medical Center, University of Freiburg, 79104 Freiburg, Germany.
4
Department of Life Sciences and Chemistry, Jacobs University Bremen, 28759 Bremen, Germany s.springer@jacobs-university.de.

Abstract

In the presence of the murine cytomegalovirus (mCMV) gp40 (m152) protein, murine major histocompatibility complex (MHC) class I molecules do not reach the cell surface but are retained in an early compartment of the secretory pathway. We find that gp40 does not impair the folding or high-affinity peptide binding of the class I molecules but binds to them, leading to their retention in the endoplasmic reticulum (ER), the ER-Golgi intermediate compartment (ERGIC) and the cis-Golgi, most likely by retrieval from the cis-Golgi to the ER. We identify a sequence in gp40 that is required for both its own retention in the early secretory pathway and for that of class I molecules.

KEYWORDS:

Antigen presentation; ERGIC and cis-Golgi retention; Early secretory pathway; Immune evasion; Murine cytomegalovirus

PMID:
26527401
DOI:
10.1242/jcs.175620
[Indexed for MEDLINE]
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