L
Lei Sun
Researcher at Pfizer
Publications - 5
Citations - 1920
Lei Sun is an academic researcher from Pfizer. The author has contributed to research in topics: MHC class I & Gene product. The author has an hindex of 5, co-authored 5 publications receiving 1883 citations.
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Journal ArticleDOI
The Human Cytomegalovirus US11 Gene Product Dislocates MHC Class I Heavy Chains from the Endoplasmic Reticulum to the Cytosol
Emmanuel J. H. J. Wiertz,Thomas R. Jones,Lei Sun,Matthew Bogyo,Hans J. Geuze,Hidde L. Ploegh +5 more
TL;DR: Human cytomegalovirus (HCMV) down-regulates expression of MHC class I products by selective proteolysis by encodes an endoplasmic reticulum resident type-I transmembrane glycoprotein, which dislocates newly synthesized class I molecules from the ER to the cytosol, where they are acted upon by an N-glycanase and the proteasome.
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Human cytomegalovirus US3 impairs transport and maturation of major histocompatibility complex class I heavy chains
Thomas R. Jones,Emmanuel J. H. J. Wiertz,Lei Sun,Kenneth N. Fish,Jay A. Nelson,Hidde L. Ploegh +5 more
TL;DR: The data suggest that gpUS3 impairs egress of MHC class I heavy chains from the endoplasmic reticulum.
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Chemokine Sequestration by Viral Chemoreceptors as a Novel Viral Escape Strategy: Withdrawal of Chemokines from the Environment of Cytomegalovirus-infected Cells
Bahram Bodaghi,Thomas R. Jones,Donato Zipeto,Claudio Vita,Lei Sun,Lysiane Laurent,Fernando Arenzana-Seisdedos,Jean-Louis Virelizier,Susan Michelson +8 more
TL;DR: Human cytomegalovirus can modify the chemokine environment of infected cells through intense sequestering of CC chemokines, mediated principally by expression of the US28-encodedChemokine receptor.
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The Human Cytomegalovirus UL97 Protein Is Phosphorylated and a Component of Virions
TL;DR: The role of pUL97 in the HCMV replication cycle, and the mechanism by which it causes phosphorylation of GCV, are currently unknown as mentioned in this paper, however, the authors of this paper have shown that pUL-97 is a virion phosphoprotein, and a likely tegument component.
Journal ArticleDOI
Inhibition of Human Cytomegalovirus UL80 Protease by Specific Intramolecular Disulfide Bond Formation
Ellen Z. Baum,Marshall M. Siegel,Geraldine Bebernitz,Jeffrey D. Hulmes,Latha Sridharan,Lei Sun,Keiko Tabei,Stuart H. Johnston,Mary Jo Wildey,John Nygaard,Thomas R. Jones,Yakov Gluzman +11 more
TL;DR: Examination of the CL13933 loading patterns of wild type and the five mutant proteases by mass spectrometry revealed that residues Cys87, Cys138, and Cys161 react with CL 13933, and that the disulfide pair partner of each is able to displace the compound via thiol-disulfide exchange.