title: Manipulation of ubiquitin/SUMO pathways in human herpesviruses infection.
abstract: Post-translational modification of proteins with ubiquitin/small ubiquitin-like modifier (SUMO) molecules triggers multiple signaling pathways that are critical for many aspects of cellular physiology. Given that viruses hijack the biosynthetic and degradative systems of their host, it is not surprising that viruses encode proteins to manipulate the host's cellular machinery for ubiquitin/SUMO modification at multiple levels. Infection with a herpesvirus, among the most ubiquitous human DNA viruses, has been linked to many human diseases, including cancers. The interplay between human herpesviruses and the ubiquitylation/SUMOylation modification system has been extensively investigated in the past decade. In this review, we present an overview of recent advances to address how the ubiquitin/SUMO-modified system alters the latency and lytic replication of herpesvirus and how herpesviruses usurp the ubiquitin/SUMO pathways against the host's intrinsic and innate immune response to favor their pathogenesis.
authors.affiliation: MOE & MOH Key Laboratory of Medical Molecular Virology, School of Basic Medicine, Shanghai Medical College, Fudan University, Shanghai, China.
authors.forename: Jin
authors.initials: J
authors.lastname: Gan
authors.affiliation: Department of Medical Systems Biology, School of Basic Medical Sciences; Department of Translational Medicine, Shanghai Public Health Clinical Center, Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
authors.forename: Niu
authors.initials: N
authors.lastname: Qiao
authors.affiliation: Department of Microbiology & Immunology, University of Nevada, Reno School of Medicine, Reno, NV, USA.
authors.forename: Roxanne
authors.initials: R
authors.lastname: Strahan
authors.affiliation: MOE & MOH Key Laboratory of Medical Molecular Virology, School of Basic Medicine, Shanghai Medical College, Fudan University, Shanghai, China.
authors.forename: Caixia
authors.initials: C
authors.lastname: Zhu
authors.affiliation: Department of Medical Systems Biology, School of Basic Medical Sciences; Department of Translational Medicine, Shanghai Public Health Clinical Center, Institutes of Biomedical Sciences, Fudan University, Shanghai, China.
authors.forename: Lei
authors.initials: L
authors.lastname: Liu
authors.affiliation: Department of Microbiology & Immunology, University of Nevada, Reno School of Medicine, Reno, NV, USA.
authors.forename: Subhash C
authors.initials: SC
authors.lastname: Verma
authors.affiliation: ShengYushou Center of Cell Biology and Immunology, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, China.
authors.forename: Fang
authors.initials: F
authors.lastname: Wei
authors.affiliation: MOE & MOH Key Laboratory of Medical Molecular Virology, School of Basic Medicine, Shanghai Medical College, Fudan University, Shanghai, China.
authors.forename: Qiliang
authors.initials: Q
authors.lastname: Cai
mesh_terms: D006564:Herpesviridae / Q000502:physiology*; D054884:Host-Pathogen Interactions; D006801:Humans; D057131:Immune Evasion; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*; D058207:Sumoylation; D025801:Ubiquitin / Q000378:metabolism*; D054875:Ubiquitination; D014779:Virus Replication
chemical_list: D025841:Small Ubiquitin-Related Modifier Proteins; D025801:Ubiquitin
keywords: SUMO; herpesvirus; ubiquitin