Article ; Online: Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein.
2020 Volume 286, Page(s) 198058
Abstract: ... of the SARS-CoV-2 contains a receptor-binding motif different from that of SARS-CoV, with some insertions ... the structural characteristics of the N-terminal domain of the S1 subunit (S1-NTD) of the SARS-CoV-2 spike ... binding abilities could be displayed by the SARS-CoV-2 S1-NTD. Moreover, concerning the origin ...
| Abstract | The 2019 novel coronavirus disease (COVID-19) that emerged in China has been declared as public health emergency of international concern by the World Health Organization and the causative pathogen was named severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this report, we analyzed the structural characteristics of the N-terminal domain of the S1 subunit (S1-NTD) of the SARS-CoV-2 spike protein in comparison to the SARS-CoV in particular, and to other viruses presenting similar characteristic in general. Given the severity and the wide and rapid spread of the SARS-CoV-2 infection, it is very likely that the virus recognizes other receptors/co-receptors besides the ACE2. The NTD of the SARS-CoV-2 contains a receptor-binding motif different from that of SARS-CoV, with some insertions that could confer to the new coronavirus new receptor binding abilities. In particular, motifs similar to the insertion 72GTNGTKR78 have been found in structural proteins of other viruses; and these motifs were located in putative regions involved in recognizing protein and sugar receptors, suggesting therefore that similar binding abilities could be displayed by the SARS-CoV-2 S1-NTD. Moreover, concerning the origin of these NTD insertions, our findings point towards an evolutionary acquisition rather than the hypothesis of an engineered virus. |
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| MeSH term(s) | Amino Acid Sequence ; Angiotensin-Converting Enzyme 2 ; Animals ; Betacoronavirus/chemistry ; Betacoronavirus/genetics ; Betacoronavirus/metabolism ; Binding Sites ; COVID-19 ; Chiroptera ; Coronavirus Infections/pathology ; Coronavirus Infections/virology ; Evolution, Molecular ; Gene Expression ; Host-Pathogen Interactions/drug effects ; Host-Pathogen Interactions/genetics ; Humans ; Middle East Respiratory Syndrome Coronavirus/chemistry ; Middle East Respiratory Syndrome Coronavirus/genetics ; Middle East Respiratory Syndrome Coronavirus/metabolism ; Models, Molecular ; Pandemics ; Peptidyl-Dipeptidase A/chemistry ; Peptidyl-Dipeptidase A/genetics ; Peptidyl-Dipeptidase A/metabolism ; Pneumonia, Viral/pathology ; Pneumonia, Viral/virology ; Protein Binding ; Protein Conformation, alpha-Helical ; Protein Conformation, beta-Strand ; Protein Interaction Domains and Motifs ; Receptors, Virus/chemistry ; Receptors, Virus/genetics ; Receptors, Virus/metabolism ; SARS Virus/chemistry ; SARS Virus/genetics ; SARS Virus/metabolism ; SARS-CoV-2 ; Sequence Alignment ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/genetics ; Spike Glycoprotein, Coronavirus/metabolism ; Structural Homology, Protein ; Thermodynamics ; Virus Attachment |
| Chemical Substances | Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Peptidyl-Dipeptidase A (EC 3.4.15.1) ; ACE2 protein, human (EC 3.4.17.23) ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) |
| Keywords | covid19 |
| Language | English |
| Publishing date | 2020-06-09 |
| Publishing country | Netherlands |
| Document type | Journal Article |
| ZDB-ID | 605780-9 |
| ISSN | 1872-7492 ; 0168-1702 |
| ISSN (online) | 1872-7492 |
| ISSN | 0168-1702 |
| DOI | 10.1016/j.virusres.2020.198058 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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