A virus that has gone viral: amino acid mutation in S protein of Indian isolate of Coronavirus COVID-19 might impact receptor binding, and thus, infectivity
Autor: | Upasana Ray, Priyanka Saha, Arup Kumar Banerjee, Prem Prakash Tripathi, Amit Kumar Srivastava |
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Rok vydání: | 2020 |
Předmět: |
Models
Molecular 0301 basic medicine viruses Pneumonia Viral Biophysics India Biology medicine.disease_cause Genome Biochemistry Virus RBD S protein Betacoronavirus 03 medical and health sciences 0302 clinical medicine Structural Biology Viral entry Virology medicine Humans Point Mutation Amino Acid Sequence Pandemics Molecular Biology Peptide sequence Research Articles Coronavirus Genetics chemistry.chemical_classification Mutation SARS-CoV-2 Point mutation COVID-19 Cell Biology Amino acid 030104 developmental biology Amino Acid Substitution SARS-CoV chemistry 030220 oncology & carcinogenesis GenBank Spike Glycoprotein Coronavirus Receptors Virus Coronavirus Infections |
Zdroj: | Bioscience Reports |
ISSN: | 1573-4935 0144-8463 |
Popis: | Since 2002, β coronaviruses (CoVs) have caused three zoonotic outbreaks, SARS-CoV in 2002, MERS-CoV in 2012, and the recent outbreak of SARS-CoV-2 late in 2019 (also named as COVID-19 or novel coronavirus 2019 or nCoV2019). Spike (S) protein, one of the structural proteins of this virus plays key role in receptor (ACE2) binding and thus virus entry. Thus, this protein has attracted scientists for detailed study and therapeutic targeting. As the nCoV2019 takes its course throughout the world, more and more sequence analyses are being done and genome sequences are being deposited in various databases. From India, two clinical isolates have been sequenced and the full genome has been deposited in GenBank. We have performed sequence analyses of the Spike protein of the Indian isolates and compared with that of the Wuhan, China (where the outbreak was first reported). While all the sequences of Wuhan isolates are identical, we found point mutations in the Indian isolates. Out of the two isolates, one was found to harbor a mutation in its receptor-binding domain (RBD) at position 407. At this site, arginine (a positively charged amino acid) was replaced by isoleucine (a hydrophobic amino acid that is also a C-β branched amino acid). This mutation has been seen to change the secondary structure of the protein at that region and this can potentially alter receptor binding of the virus. Although this finding needs further validation and more sequencing, the information might be useful in rational drug designing and vaccine engineering. |
Databáze: | OpenAIRE |
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