tetano
Editor, Senior Moderator
Curr Res Microb Sci
. 2020 Sep;1:53-61.
doi: 10.1016/j.crmicr.2020.06.003. Epub 2020 Jun 29.
Minireview of progress in the structural study of SARS-CoV-2 proteins
Guoliang Zhu[SUP] 1 2 [/SUP], Chunmei Zhu[SUP] 1 2 [/SUP], Yun Zhu[SUP] 1 [/SUP], Fei Sun[SUP] 1 [/SUP]
Affiliations
Abstract
A severe form of pneumonia, named coronavirus disease 2019 (COVID-19) by the World Health Organization, broke out in China and rapidly developed into a global pandemic, with millions of cases and hundreds of thousands of deaths reported globally. The novel coronavirus, which was designated as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was identified as the etiological agent of COVID-19. On the basis of experience accumulated following previous SARS-CoV and MERS-CoV outbreaks and research, a series of studies have been conducted rapidly, and major progress has been achieved with regard to the understanding of the phylogeny and genomic organization of SARS-CoV-2 in addition its molecular mechanisms of infection and replication. In the present review, we summarized crucial developments in the elucidation of the structure and function of key SARS-CoV-2 proteins, especially the main protease, RNA-dependent RNA polymerase, spike glycoprotein, and nucleocapsid protein. Results of studies on their associated inhibitors and drugs have also been highlighted.
Keywords: 3CLpro, 3C-like protease; 6-HB, six-helix bundle; ACE2, angiotensin-converting enzyme 2; COVID-19; COVID-19, coronavirus disease 2019; CatB/L, cysteine proteases-cathepsin B and L; Drug-screening; E protein, Envelope protein; Genome-encoded proteins; HR1, heptad repeat 1; HR2, heptad repeat 2; M protein, Membrane protein; MERS-CoV, the Middle Eastern respiratory syndrome coronavirus; Mpro, Main protease; N protein, Nucleocapsid protein; NSP, non-structural protein; ORF, Open reading frame; PD, peptidase domain; RBD, receptor-binding domain; RBM, receptor-binding motif; RMP, The remdesivir monophosphate; RdRp, RNA-dependent RNA polymerase; S protein, Spike glycoprotein; SARS-CoV, severe acute respiratory syndrome coronavirus; SARS-CoV-2; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; Structure-based screening; gRNA, genomic RNA; sgRNA, subgenomic RNA.
. 2020 Sep;1:53-61.
doi: 10.1016/j.crmicr.2020.06.003. Epub 2020 Jun 29.
Minireview of progress in the structural study of SARS-CoV-2 proteins
Guoliang Zhu[SUP] 1 2 [/SUP], Chunmei Zhu[SUP] 1 2 [/SUP], Yun Zhu[SUP] 1 [/SUP], Fei Sun[SUP] 1 [/SUP]
Affiliations
- PMID: 33236001
- PMCID: PMC7323663
- DOI: 10.1016/j.crmicr.2020.06.003
Abstract
A severe form of pneumonia, named coronavirus disease 2019 (COVID-19) by the World Health Organization, broke out in China and rapidly developed into a global pandemic, with millions of cases and hundreds of thousands of deaths reported globally. The novel coronavirus, which was designated as severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), was identified as the etiological agent of COVID-19. On the basis of experience accumulated following previous SARS-CoV and MERS-CoV outbreaks and research, a series of studies have been conducted rapidly, and major progress has been achieved with regard to the understanding of the phylogeny and genomic organization of SARS-CoV-2 in addition its molecular mechanisms of infection and replication. In the present review, we summarized crucial developments in the elucidation of the structure and function of key SARS-CoV-2 proteins, especially the main protease, RNA-dependent RNA polymerase, spike glycoprotein, and nucleocapsid protein. Results of studies on their associated inhibitors and drugs have also been highlighted.
Keywords: 3CLpro, 3C-like protease; 6-HB, six-helix bundle; ACE2, angiotensin-converting enzyme 2; COVID-19; COVID-19, coronavirus disease 2019; CatB/L, cysteine proteases-cathepsin B and L; Drug-screening; E protein, Envelope protein; Genome-encoded proteins; HR1, heptad repeat 1; HR2, heptad repeat 2; M protein, Membrane protein; MERS-CoV, the Middle Eastern respiratory syndrome coronavirus; Mpro, Main protease; N protein, Nucleocapsid protein; NSP, non-structural protein; ORF, Open reading frame; PD, peptidase domain; RBD, receptor-binding domain; RBM, receptor-binding motif; RMP, The remdesivir monophosphate; RdRp, RNA-dependent RNA polymerase; S protein, Spike glycoprotein; SARS-CoV, severe acute respiratory syndrome coronavirus; SARS-CoV-2; SARS-CoV-2, severe acute respiratory syndrome coronavirus 2; Structure-based screening; gRNA, genomic RNA; sgRNA, subgenomic RNA.