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. 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

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The Murine Cytomegalovirus Immunoevasin gp40 Binds MHC Class I Molecules to Retain Them in the Early Secretory Pathway

Linda Janßen et al. J Cell Sci. .
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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.

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