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Extensive genetic diversity with novel mutations in spike glycoprotein of severe acute respiratory syndrome coronavirus 2, Bangladesh in late 2020.
Afrin, S Z; Paul, S K; Begum, J A; Nasreen, S A; Ahmed, S; Ahmad, F U; Aziz, M A; Parvin, R; Aung, M S; Kobayashi, N.
  • Afrin SZ; Department of Microbiology, Mymensingh Medical College, Mymensingh, Bangladesh.
  • Paul SK; Department of Microbiology, Netrokona Medical College, Netrokona, Bangladesh.
  • Begum JA; Department of Pathology, Faculty of Veterinary Science, Bangladesh Agricultural University, Mymensingh, Bangladesh.
  • Nasreen SA; Department of Microbiology, Mymensingh Medical College, Mymensingh, Bangladesh.
  • Ahmed S; Department of Microbiology, Mymensingh Medical College, Mymensingh, Bangladesh.
  • Ahmad FU; Department of Microbiology, TMSS Medical College, Bogura, Bangladesh.
  • Aziz MA; Department of Microbiology, Rangpur Medical College, Rangpur, Bangladesh.
  • Parvin R; Department of Pathology, Faculty of Veterinary Science, Bangladesh Agricultural University, Mymensingh, Bangladesh.
  • Aung MS; Department of Hygiene, Sapporo Medical University School of Medicine, Sapporo, Japan.
  • Kobayashi N; Department of Hygiene, Sapporo Medical University School of Medicine, Sapporo, Japan.
New Microbes New Infect ; 41: 100889, 2021 May.
Article in English | MEDLINE | ID: covidwho-1289741
ABSTRACT
In Bangladesh, coronavirus disease 2019 (COVID-19) has been highly prevalent during late 2020, with nearly 500 000 confirmed cases. In the present study, the spike (S) protein of severe acute respiratory coronavirus 2 (SARS-CoV-2) circulating in Bangladesh was genetically investigated to elucidate the diversity of mutations and their prevalence. The nucleotide sequence of the S protein gene was determined for 15 SARS-CoV-2 samples collected from eight divisions in Bangladesh, and analysed for mutations compared with the reference strain (hCoV-19/Wuhan/WIV04/2019). All the SARS-CoV-2 S genes were assigned to B.1 lineage in G clade, and individual S proteins had 1-25 mutations causing amino acid substitution/deletion. A total of 133 mutations were detected in 15 samples, with D614G being present in all the samples; 53 were novel mutations as of January 2021. On the receptor-binding domain, 21 substitutions including ten novel mutations were identified. Other novel mutations were located on the N-terminal domain (S1 subunit) and dispersed sites in the S2 subunit, including two substitutions that remove potential N-glycosylation sites. A P681R substitution adjacent to the furin cleavage site was detected in one sample. All the mutations detected were located on positions that are functionally linked to host transition, antigenic drift, host surface receptor binding or antibody recognition sites, and viral oligomerization interfaces, which presumably related to viral transmission and pathogenic capacity.
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Full text: Available Collection: International databases Database: MEDLINE Type of study: Observational study Language: English Journal: New Microbes New Infect Year: 2021 Document Type: Article Affiliation country: J.nmni.2021.100889

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Full text: Available Collection: International databases Database: MEDLINE Type of study: Observational study Language: English Journal: New Microbes New Infect Year: 2021 Document Type: Article Affiliation country: J.nmni.2021.100889