Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions

Ujike, Makoto; Taguchi, Fumihiro

doi:10.3390/v7041700

Cited by 140 publications

(162 citation statements)

References 127 publications

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“…Virion assembly is triggered by the action of the M protein, which assists in incorporating the nucleocapsid, the envelope and the spike into virus particles. Budding takes place between the endoplasmic reticulum and the Golgi and new viruses are released by exocytosis (McBride et al, 2014;Neuman et al, 2011;Ruch and Machamer, 2012;Ujike and Taguchi, 2015).…”

Section: The Coronavirus Genomementioning

confidence: 99%

Interaction of SARS and MERS Coronaviruses with the Antiviral Interferon Response

Kindler

Thiel

Weber

2016

Advances in Virus Research

276

265

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Section: The Coronavirus Genomementioning

confidence: 99%

Interaction of SARS and MERS Coronaviruses with the Antiviral Interferon Response

Kindler

Thiel

Weber

2016

Advances in Virus Research

276

265

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“…In eukaryotes, secretory proteins, such as transmembrane proteins destined for the plasma membrane and the lysosome, are synthesised in the rough endoplasmic reticulum. These proteins are then delivered to the endoplasmic reticulum (ER)–Golgi intermediate compartment (ERGIC), a membrane compartment between ER and Golgi for cargo sorting and recycling, in a manner dependent on the coat protein II complex (Johnson et al., ; Ujike and Taguchi, ). Though the role of coat protein I (COPI) at the ERGIC remains controversial, it was proposed that mobile TCs coated by COPI complexes deliver cargo to the Golgi (Brandizzi and Barlowe, ).…”

Section: Overview Of Membrane Trafficking From the Tgn Towards The Enmentioning

confidence: 99%

Cargo trafficking from the trans‐Golgi network towards the endosome

Gadila

Kim

2016

Biology of the Cell

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The trans-Golgi network (TGN) is a major sorting, packing and delivering station of newly synthesised proteins and lipids to their final destination. These cargo molecules follow the secretory pathway, which is a vital part of cellular trafficking machinery in all eukaryotic cells. This secretory pathway is well conserved in all eukaryotes from low-level eukaryotes, such as yeast, to higher level eukaryotes like mammals. The molecular mechanisms of protein sorting by adaptor proteins, membrane elongation and transport to the final destinations by motor proteins and the cytoskeleton, and membrane pinching-off by scission proteins must be choreographically managed for efficient cargo delivery, and the understanding of these detailed processes is not yet completed. Functionally, defects in these mechanisms are associated with the pathology of prominent diseases such as acute myeloid leukaemia, Charcot-Marie-Tooth disease, I-cell disease and Wiskott-Aldrich syndrome. The present review points out the recent advances in our knowledge of the molecular mechanisms involved in the transportation of the cargo from the TGN towards the endosome.

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“…Viral envelope comprises of three proteins where spike (S) and membrane (M) are the two major glycoproteins and envelope (E) is the non-glycosylated protein. The M protein comprises of short N-terminal glycosylated ectodomain with three transmembrane domains (TM) and a long C-terminal CT domain [12]. The M and E proteins are required for virus morphogenesis, assembly and budding.…”

Section: Introductionmentioning

confidence: 99%

Structural, glycosylation and antigenic variation between 2019 novel coronavirus (2019-nCoV) and SARS coronavirus (SARS-CoV)

et al. 2020

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The emergence of 2019 novel coronavirus (2019-nCoV) is of global concern and might have emerged from RNA recombination among existing coronaviruses. CoV spike (S) protein which is crucial for receptor binding, membrane fusion via conformational changes, internalization of the virus, host tissue tropism and comprises crucial targets for vaccine development, remain largely uncharacterized. Therefore, the present study has been planned to determine the sequence variation, structural and antigenic divergence of S glycoprotein which may be helpful for the management of 2019-nCoV infection. The sequences of spike glycoprotein of 2019-nCoV and SARS coronavirus (SARS-CoV) were used for the comparison. The sequence variations were determined using EMBOSS Needle pairwise sequence alignment tools. The variation in glycosylation sites was predicted by NetNGlyc 1.0 and validated by N-GlyDE server. Antigenicity was predicted by NetCTL 1.2 and validated by IEDB Analysis Resource server. The structural divergence was determined by using SuperPose Version 1.0 based on cryo-EM structure of the SARS coronavirus spike glycoprotein. Our data suggests that 2019-nCoV is newly spilled coronavirus into humans in China is closely related to SARS-CoV, which has only 12.8% of difference with SARS-CoV in S protein and has 83.9% similarity in minimal receptor-binding domain with SARS-CoV. Addition of a novel glycosylation sites were observed in 2019-nCoV. In addition, antigenic analysis proposes that great antigenic differences exist between both the viral strains, but some of the epitopes were found to be similar between both the S proteins. In spite of the variation in S protein amino acid composition, we found no significant difference in their structures. Collectively, for the first time our results exhibit the emergence of human 2019-nCoV is closely related to predecessor SARS-CoV and provide the evidence that 2019-nCoV uses various novel glycosylation sites as SARS-CoV and may have a potential to become pandemic owing its antigenic discrepancy. Further, demonstration of novel Cytotoxic T lymphocyte epitopes may impart opportunities for the development of peptide based vaccine for the prevention of 2019-nCoV.

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Incorporation of Spike and Membrane Glycoproteins into Coronavirus Virions

Cited by 140 publications

References 127 publications

Interaction of SARS and MERS Coronaviruses with the Antiviral Interferon Response

Interaction of SARS and MERS Coronaviruses with the Antiviral Interferon Response

Cargo trafficking from the trans‐Golgi network towards the endosome

Structural, glycosylation and antigenic variation between 2019 novel coronavirus (2019-nCoV) and SARS coronavirus (SARS-CoV)

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