About: Proteomic analysis on structural proteins of Severe Acute Respiratory Syndrome coronavirus

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Proteomic analysis on structural proteins of Severe Acute Respiratory Syndrome coronavirus
Creator	Liu, Hong Cao, Cheng Li, Weihua Sun, Wei Wang, Jie Chang, Guohui Peng, Wenming Qin, Ede Yu, Man Zhu, Qingyu Wang, Jinglan He, Fuchu Li, Dong Chen, Tinggui Zhang, Xuemin Wan, Ping Shi, Rong Dong, Fangting Kuai, Xuezhang Dai, Jingquan Li, Xiaohai Qian, Xiaohong Wan, Jia Wei, Handong Wu, Songfeng Ying, Wantao Zhu, Yunping Cai, Yun Dai, Shujia Du, Chunjuan Guo, Lihai Hao, Yunwei Li, Jianqi Wang, Donggen Wei, Kaihua Zhang, Yangjun
Source	Medline; PMC
abstract	Recently, a new coronavirus was isolated from the lung tissue of autopsy sample and nasal/throat swabs of the patients with Severe Acute Respiratory Syndrome (SARS) and the causative association with SARS was determined. To reveal further the characteristics of the virus and to provide insight about the molecular mechanism of SARS etiology, a proteomic strategy was utilized to identify the structural proteins of SARS coronavirus (SARS‐CoV) isolated from Vero E6 cells infected with the BJ‐01 strain of the virus. At first, Western blotting with the convalescent sera from SARS patients demonstrated that there were various structural proteins of SARS‐CoV in the cultured supernatant of virus infected‐Vero E6 cells and that nucleocaspid (N) protein had a prominent immunogenicity to the convalescent sera from the patients with SARS, while the immune response of spike (S) protein probably binding with membrane (M) glycoprotein was much weaker. Then, sodium dodecyl sulfate‐polyacrylamide gel electrophoresis (SDS‐PAGE) was used to separate the complex protein constituents, and the strategy of continuous slicing from loading well to the bottom of the gels was utilized to search thoroughly the structural proteins of the virus. The proteins in sliced slots were trypsinized in‐gel and identified by mass spectrometry. Three structural proteins named S, N and M proteins of SARS‐CoV were uncovered with the sequence coverage of 38.9, 93.1 and 28.1% respectively. Glycosylation modification in S protein was also analyzed and four glycosylation sites were discovered by comparing the mass spectra before and after deglycosylation of the peptides with PNGase F digestion. Matrix‐assisted laser desorption/ionization‐mass spectrometry determination showed that relative molecular weight of intact N protein is 45 929 Da, which is very close to its theoretically calculated molecular weight 45 935 Da based on the amino acid sequence deduced from the genome with the first amino acid methionine at the N‐terminus depleted and second, serine, acetylated, indicating that phosphorylation does not happen at all in the predicted phosphorylation sites within infected cells nor in virus particles. Intriguingly, a series of shorter isoforms of N protein was observed by SDS‐PAGE and identified by mass spectrometry characterization. For further confirmation of this phenomenon and its related mechanism, recombinant N protein of SARS‐CoV was cleaved in vitro by caspase‐3 and ‐6 respectively. The results demonstrated that these shorter isoforms could be the products from cleavage of caspase‐3 rather than that of caspase‐6. Further, the relationship between the caspase cleavage and the viral infection to the host cell is discussed.
has issue date	2004-01-15(xsd:dateTime)
bibo:doi	10.1002/pmic.200300676
bibo:pmid	14760722
has license	no-cc
sha1sum (hex)	2cf44d7a50d3a18ee0369c92acc661d517ee7a97
schema:url	https://doi.org/10.1002/pmic.200300676
resource representing a document's title	Proteomic analysis on structural proteins of Severe Acute Respiratory Syndrome coronavirus
has PubMed Central identifier	PMC7168022
has PubMed identifier	14760722
schema:publication	Proteomics
resource representing a document's body	covid:2cf44d7a50d3a18ee0369c92acc661d517ee7a97#body_text
is schema:about of	named entity 'proteins' named entity 'sequence' named entity 'shorter' named entity 'immunogenicity' named entity 'mechanism' named entity 'relative' named entity 'host' named entity 'identify' named entity 'virus' named entity 'IN S' named entity 'SWABS' named entity 'PAGE' named entity 'THESE' named entity 'IN VITRO' named entity 'DOES NOT' named entity 'WESTERN BLOTTING' named entity 'MHV' named entity 'INFECTED' named entity 'PHOSPHORYLATION SITES' named entity 'IMMUNE RESPONSE' named entity 'MECHANISM' named entity 'PROTEIN' named entity 'COMPLEX PROTEIN' named entity 'MODIFICATION' named entity 'PATIENTS' named entity 'SUPERNATANT' named entity 'S PROTEIN' named entity 'CULTURED' named entity 'CONVALESCENT' named entity 'UNCOVERED' named entity 'NAMED' named entity 'PHOSPHORYLATION' named entity 'CALCULATED' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME' named entity 'RELATIVE' named entity 'CORONAVIRUS' named entity 'DEPLETED' named entity 'RESULTS' named entity 'SAMPLE' named entity 'ABBREVIATIONS' named entity 'M PROTEINS' named entity 'VIRUS' named entity 'INTACT' named entity 'INDICATING' named entity 'INSIGHT' named entity 'SPIKE'

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