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Title: The murine cytomegalovirus immunoevasin gp40 binds MHC class I molecules to retain them in the early secretory pathway. Author: Janßen L, Ramnarayan VR, Aboelmagd M, Iliopoulou M, Hein Z, Majoul I, Fritzsche S, Halenius A, Springer S. Journal: J Cell Sci; 2016 Jan 01; 129(1):219-27. PubMed ID: 26527401. 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.[Abstract] [Full Text] [Related] [New Search]