共 202 条
Post-translational modifications of coronavirus proteins: roles and function
被引:154
作者:
Fung, To Sing
[1
,2
]
Liu, Ding Xiang
[1
,2
,3
]
机构:
[1] South China Agr Univ, Guangdong Prov Key Lab Microbial Signals & Dis Co, Guangzhou 510642, Guangdong, Peoples R China
[2] Integrat Microbiol Res Ctr, Guangzhou 510642, Guangdong, Peoples R China
[3] Nanyang Technol Univ, Sch Biol Sci, 60 Nanyang Dr, Singapore 637551, Singapore
关键词:
coronavirus;
deubiquitination;
glycosylation;
innate immunity;
pathogenesis;
phosphorylation;
post-translational modification;
replication;
ubiquitination;
virus-host interaction;
RESPIRATORY SYNDROME-CORONAVIRUS;
INFECTIOUS-BRONCHITIS-VIRUS;
PAPAIN-LIKE PROTEASE;
MOUSE HEPATITIS-VIRUS;
TRANSMISSIBLE GASTROENTERITIS VIRUS;
N-LINKED GLYCOSYLATION;
CELL-CELL FUSION;
SARS-CORONAVIRUS;
NUCLEOCAPSID PROTEIN;
SPIKE PROTEIN;
D O I:
10.2217/fvl-2018-0008
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
Post-translational modifications (PTMs) refer to the covalent modifications of polypeptides after they are synthesized, adding temporal and spatial regulation to modulate protein functions. Being obligate intracellular parasites, viruses rely on the protein synthesis machinery of host cells to support replication, and not surprisingly, many viral proteins are subjected to PTMs. Coronavirus (CoV) is a group of enveloped RNA viruses causing diseases in both human and animals. Many CoV proteins are modified by PTMs, including glycosylation and palmitoylation of the spike and envelope protein, N- or O-linked glycosylation of the membrane protein, phosphorylation and ADP-ribosylation of the nucleocapsid protein, and other PTMs on nonstructural and accessory proteins. In this review, we summarize the current knowledge on PTMs of CoV proteins, with an emphasis on their impact on viral replication and pathogenesis. The ability of some CoV proteins to interfere with PTMs of host proteins will also be discussed.
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页码:405 / 430
页数:26
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