Corpus overview


MeSH Disease

HGNC Genes

SARS-CoV-2 proteins

ProteinN (1)

ProteinS (1)


SARS-CoV-2 Proteins
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    SARS-CoV-2 Nucleocapsid protein PROTEIN is decorated with multiple N- and O-glycans.

    Authors: Nitin T Supekar; Asif Shajahan; Anne Gleinich; Daniel Rouhani; Christian Heiss; Parastoo Azadi; Peter van Run; Geert van Amerongen; Leon de Waal; Marion Koopmans; Koert J Stittelaar; Judith van den Brand; Bart L Haagmans; Lun Zhang; Sheng-jie Hou; Xiao-lin Yu; Yu-ling Wang; Hui-xia Gao; Xue-han Shi; Chang-wen Ke; Bi-xia Ke; Chun-guo Jiang; Rui-tian Liu; Rodney Daniels; John McCauley; Pramila Rijal; Alain Townsend

    doi:10.1101/2020.08.26.269043 Date: 2020-08-27 Source: bioRxiv

    Severe acute respiratory syndrome coronavirus 2 MESHD (SARS-CoV-2), which causes coronavirus disease MESHD ( COVID-19 MESHD) started at the end of 2019 in Wuhan, China has spread rapidly and became a pandemic. Since there is no therapy available that is proven as fully protective against COVID-19 MESHD, a vaccine to protect against deadly COVID-19 MESHD is urgently needed. Nucleocapsid protein (N PROTEIN protein), is one of the most abundant proteins in coronaviruses and is a potential target for both vaccine development and point of care diagnostics. The variable mass of N protein PROTEIN (45 to 60 kDa), suggests the presence of post-translational modifications ( PTMs HGNC), and it is critical to clearly define these PTMs HGNC to gain the structural understanding necessary for further vaccine research. There have been several reports suggesting that the N protein PROTEIN is phosphorylated but lacks glycosylation. Our comprehensive glycomics and glycoproteomics experiments confirm that the N protein PROTEIN is highly O-glycosylated and also contains significant levels of N-glycosylation. We were able to confirm the presence of O-glycans on seven sites with substantial glycan occupancy, in addition to less abundant O-glycans on four sites. We also detected N-glycans on two out of five potential N-glycosylation sites. Moreover, we were able to confirm one phosphorylation site. Recent studies have indicated that the N protein PROTEIN can serve as an important diagnostic marker for coronavirus disease MESHD and a major immunogen by priming protective immune responses. Thus, detailed structural characterization of the N protein PROTEIN may provide useful insights for understanding the roles of glycosylation on viral pathogenesis and also in vaccine design and development.

    Mass spectrometry analysis of newly emerging coronavirus HCoV-19 spike S protein PROTEIN and human ACE2 HGNC reveals camouflaging glycans and unique post-translational modifications

    Authors: Zeyu Sun; Keyi Ren; Xing Zhang; Jinghua Chen; Zhengyi Jiang; Jing Jiang; Feiyang Ji; Xiaoxi Ouyang; Lanjuan Li

    doi:10.1101/2020.04.29.068098 Date: 2020-04-29 Source: bioRxiv

    The pneumonia-causing COVID-19 MESHD pandemia has prompt worldwide efforts to understand its biological and clinical traits of newly identified HCoV-19 virus. In this study, post-translational modification (PTM) of recombinant HCoV-19 S and hACE2 HGNC were characterized by LC-MSMS. We revealed that both proteins were highly decorated with specific proportions of N-glycan subtypes. Out of 21 possible glycosites in HCoV-19 S protein PROTEIN, 20 were confirmed completely occupied by N-glycans, with oligomannose glycans being the most abundant type. All 7 possible glycosylation sites in hACE2 HGNC were completely occupied mainly by complex type N-glycans. However, we showed that glycosylation did not directly contribute to the binding affinity between SARS-CoV spike MESHD spike protein PROTEIN and hACE2 HGNC. Additionally, we also identified multiple sites methylated in both proteins, and multiple prolines in hACE2 HGNC were converted to hydroxylproline. Refined structural models were built by adding N-glycan and PTMs HGNC to recently published cryo-EM structure of the HCoV-19 S and hACE2 HGNC generated with glycosylation sites in the vicinity of binding surface. The PTM and glycan maps of both HCoV-19 S and hACE2 HGNC provide additional structural details to study mechanisms underlying host attachment, immune response mediated by S protein PROTEIN and hACE2 HGNC, as well as knowledge to develop remedies and vaccines desperately needed nowadays.

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MeSH Disease
HGNC Genes
SARS-CoV-2 Proteins

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