The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Hu, Yu‐Chen; Wen, Jin‐Kun; Tang, Lin; Zhang, Haijun; Zhang, Xiaowei; Li, Yan; Wang, Jing; Han, Yujun; Li, Guoqing; Shi, Jianping; Tian, Xin; Jiang, Feng; Zhao, Xiaoqian; Wang, Jun; Liu, Siqi; Zeng, Changqing; Wang, Jian; Yang, Huanming

doi:10.1016/s1672-0229(03)01016-7

Cited by 75 publications

(57 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1a). The Asn-Gly-Thr (a.a. 4-6) at the N-terminal of SARS-CoV M protein is a defined consensus sequence (Asn-X-(Ser/Thr)) for N-linked glycosylation [21]. This is verified by the observation that production of the glycosylated M protein was blocked when amino acid residue 4 was changed from Asn (lane 2 in Fig.…”

Section: Sars-cov M Protein Is An N-glycosylated Proteinmentioning

confidence: 63%

Expression and membrane integration of SARS-CoV M protein

et al. 2008

View full text Add to dashboard Cite

SARS-CoV M gene fragment was cloned and expressed as a recombinant protein fused with a V5 tag at the C-terminus in Vero E6 cells. In addition to un-glycosylated and glycosylated proteins, one product with smaller size initiated in-frame from the third Met residues probably through ribosomal re-initiation was also detected. Translation initiated in-frame from the third Met is unusual since the sequence around the first Met of SARS-CoV M protein contains the optimal consensus Kozak sequence. The function of this smaller translated product awaits further investigation. Similar to other N-glycosylated proteins, glycosylation of SARS-CoV M protein was occurred co-translationally in the presence of microsomes. The SARS-CoV M protein is predicted as a triple-spanning membrane protein lack of a conventional signal peptide. The second and third trans-membrane regions (a.a. 46-68 and 78-100) are predicted to be the primary type helices, which will be able to penetrate into membrane by themselves, while the first trans-membrane region (a.a. 14-36) is predicted to be the secondary type helix, which is considered to be stabilized by the interaction with other trans-membrane segments. As expected, the second and third trans-membrane regions were able to insert a cytoplasmic protein into the endoplasmic reticulum membrane more efficiently than the first one. These results should be important for the study of SARS-CoV morphogenesis.

show abstract

Section: Sars-cov M Protein Is An N-glycosylated Proteinmentioning

confidence: 63%

Expression and membrane integration of SARS-CoV M protein

et al. 2008

View full text Add to dashboard Cite

show abstract

“…While the M protein of some lineage A Betacoronaviruses is O-linked glycosylated, those of other coronaviruses are exclusively Nlinked (Fung and Liu, 2018). Only a single N-glycosylation site has been identified in the SARS-CoV M protein at N4 (Hu et al, 2003;Voss et al, 2006). When expressed alone with a C-terminal FLAG-tag, SARS-CoV M protein acquired high-mannose N-glycans in the ER, which were modified into complex glycans in the Golgi (Nal et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

N-Linked glycosylation of the membrane protein ectodomain regulates infectious bronchitis virus-induced ER stress response, apoptosis and pathogenesis

et al. 2019

View full text Add to dashboard Cite

A B S T R A C TCoronavirus membrane (M) protein is the most abundant structural protein playing a critical role in virion assembly. Previous studies show that the N-terminal ectodomain of M protein is modified by glycosylation, but its precise functions are yet to be thoroughly investigated. In this study, we confirm that N-linked glycosylation occurs at two predicted sites in the M protein ectodomain of infectious bronchitis coronavirus (IBV). Dual mutations at the two sites (N3D/N6D) did not affect particle assembly, virus-like particle formation and viral replication in culture cells. However, activation of the ER stress response was significantly reduced in cells infected with rN3D/N6D, correlated with a lower level of apoptosis and reduced production of pro-inflammatory cytokines. Taken together, this study demonstrates that although not essential for replication, glycosylation in the IBV M protein ectodomain plays important roles in activating ER stress, apoptosis and proinflammatory response, and may contribute to the pathogenesis of IBV.

show abstract

“…Its hydrophilic domain is believed to interact with the nucleocapsid protein and is located inside the virus particle ( 12 ). Linear epitope mapping of the M protein using synthetic peptides revealed that amino acid residues 2,137-2,158 interacted with SARS patient sera by ELISA assay, implying the potential capability of the M protein to induce immune response 34., 35..…”

Section: Molecular Biology Of Sars-covmentioning

confidence: 99%

Molecular Advances in Severe Acute Respiratory Syndrome-Associated Coronavirus (SARS-CoV)

Chow

Hon

Hui

et al. 2003

Genomics, Proteomics &Amp; Bioinformatics

View full text Add to dashboard Cite

The sudden outbreak of severe acute respiratory syndrome (SARS) in 2002 prompted the establishment of a global scientific network subsuming most of the traditional rivalries in the competitive field of virology. Within months of the SARS outbreak, collaborative work revealed the identity of the disastrous pathogen as SARS-associated coronavirus (SARS-CoV). However, although the rapid identification of the agent represented an important breakthrough, our understanding of the deadly virus remains limited. Detailed biological knowledge is crucial for the development of effective countermeasures, diagnostic tests, vaccines and antiviral drugs against the SARS-CoV. This article reviews the present state of molecular knowledge about SARS-CoV, from the aspects of comparative genomics, molecular biology of viral genes, evolution, and epidemiology, and describes the diagnostic tests and the anti-viral drugs derived so far based on the available molecular information.

show abstract

The M Protein of SARS-CoV: Basic Structural and Immunological Properties

Cited by 75 publications

References 13 publications

Expression and membrane integration of SARS-CoV M protein

Expression and membrane integration of SARS-CoV M protein

N-Linked glycosylation of the membrane protein ectodomain regulates infectious bronchitis virus-induced ER stress response, apoptosis and pathogenesis

Molecular Advances in Severe Acute Respiratory Syndrome-Associated Coronavirus (SARS-CoV)

Contact Info

Product

Resources

About