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

Linda Janßen; Venkat Raman Ramnarayan; Mohamed Aboelmagd; Maro Iliopoulou; Zeynep Hein; Irina Majoul; Susanne Fritzsche; Anne Halenius; Sebastian Springer

doi:10.1242/jcs.175620

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

Linda Janßen, Venkat Raman Ramnarayan, Mohamed Aboelmagd, Maro Iliopoulou, Zeynep Hein, Irina Majoul, Susanne Fritzsche, Anne Halenius, Sebastian Springer^*

^*Corresponding author for this work

Institute of Biology

1 Citation (Scopus)

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.

Original language	English
Journal	Journal of Cell Science
Volume	129
Issue number	1
Pages (from-to)	219-227
Number of pages	9
ISSN	0021-9533
DOIs	https://doi.org/10.1242/jcs.175620
Publication status	Published - 01.01.2016

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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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.",

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AU - Janßen, Linda

AU - Ramnarayan, Venkat Raman

AU - Aboelmagd, Mohamed

AU - Iliopoulou, Maro

AU - Hein, Zeynep

AU - Majoul, Irina

AU - Fritzsche, Susanne

AU - Halenius, Anne

AU - Springer, Sebastian

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N2 - 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.

AB - 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.

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

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