N-terminal domain of SARS CoV-2 spike protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals

doi:10.1002/jmv.27181

. 2021 Oct;93(10):5726-5728.

doi: 10.1002/jmv.27181. Epub 2021 Jul 14.

N-terminal domain of SARS CoV-2 spike protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals

Yogendra Singh¹, Neeraj Kumar Fuloria², Shivkanya Fuloria², Vetriselvan Subramaniyan³, Dhanalekshmi Unnikrishnan Meenakshi⁴, Srikumar Chakravarthi³, Usha Kumari⁵, Navneet Joshi⁶, Gaurav Gupta⁷

Affiliations

¹ Department of Pharmacology, Maharishi Arvind College of Pharmacy, Ambabari, Jaipur, Rajasthan, India.
² Faculty of Pharmacy, AIMST University, Bedong, Kedah, Malaysia.
³ Faculty of Medicine, Bioscience and Nursing, MAHSA University, Jenjarom, Selangor, Malaysia.
⁴ College of Pharmacy, National University of Science and Technology, Muscat, Oman.
⁵ Faculty of Medicine, AIMST University, Bedong, Kedah, Malaysia.
⁶ Department of Biosciences, School of Liberal Arts and Sciences, Mody University of Science and Technology, Lakshmangarh, Sikar, Rajasthan, India.
⁷ Department of Pharmacology, School of Pharmacy, Suresh Gyan Vihar University, Jaipur, Rajasthan, India.

PMID: 34232521
PMCID: PMC8426848
DOI: 10.1002/jmv.27181

N-terminal domain of SARS CoV-2 spike protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals

Yogendra Singh et al. J Med Virol. 2021 Oct.

. 2021 Oct;93(10):5726-5728.

doi: 10.1002/jmv.27181. Epub 2021 Jul 14.

Authors

Affiliations

¹ Department of Pharmacology, Maharishi Arvind College of Pharmacy, Ambabari, Jaipur, Rajasthan, India.
² Faculty of Pharmacy, AIMST University, Bedong, Kedah, Malaysia.
³ Faculty of Medicine, Bioscience and Nursing, MAHSA University, Jenjarom, Selangor, Malaysia.
⁴ College of Pharmacy, National University of Science and Technology, Muscat, Oman.
⁵ Faculty of Medicine, AIMST University, Bedong, Kedah, Malaysia.
⁶ Department of Biosciences, School of Liberal Arts and Sciences, Mody University of Science and Technology, Lakshmangarh, Sikar, Rajasthan, India.
⁷ Department of Pharmacology, School of Pharmacy, Suresh Gyan Vihar University, Jaipur, Rajasthan, India.

PMID: 34232521
PMCID: PMC8426848
DOI: 10.1002/jmv.27181

No abstract available

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Conflict of interest statement

The authors declare that there are no conflict of interests.

Figures

**Figure 1**
N‐terminal domain of SARS CoV‐2 Spike (S) protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals and SARS‐CoV‐2‐reactive T cell‐based adoptive cellular immunotherapy of COVID‐19 infection

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References

1. Wang S, Qiu Z, Hou Y, et al. AXL is a candidate receptor for SARS‐CoV‐2 that promotes infection of pulmonary and bronchial epithelial cells. Cell Res. 2021;31(2):126‐140. - PMC - PubMed
1. Kwarteng A, Asiedu E, Sylverken AA, Larbi A, Sakyi SA, Asiedu SO. Molecular characterization of interactions between the D614G variant of SARS‐CoV‐2 S‐protein and neutralizing antibodies: A computational approach. Infect Genet Evol. 2021;91:104815. - PMC - PubMed
1. Li Q, Wu J, Nie J, et al. The impact of mutations in SARS‐CoV‐2 spike on viral infectivity and antigenicity. Cell. 2020;182(5):1284‐1294.e1289. - PMC - PubMed
1. Ke Z, Oton J, Qu K, et al. Structures and distributions of SARS‐CoV‐2 spike proteins on intact virions. Nature. 2020;588(7838):498‐502. - PMC - PubMed
1. Hodcroft EB, Domman DB, Snyder DJ, et al. Emergence in late 2020 of multiple lineages of SARS‐CoV‐2 Spike protein variants affecting amino acid position 677. medRxiv. 2021;2021. 10.1101/2021.02.12.21251658 - DOI

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[1] Wang S, Qiu Z, Hou Y, et al. AXL is a candidate receptor for SARS‐CoV‐2 that promotes infection of pulmonary and bronchial epithelial cells. Cell Res. 2021;31(2):126‐140. - PMC - PubMed

[2] Wang S, Qiu Z, Hou Y, et al. AXL is a candidate receptor for SARS‐CoV‐2 that promotes infection of pulmonary and bronchial epithelial cells. Cell Res. 2021;31(2):126‐140. - PMC - PubMed

[3] Kwarteng A, Asiedu E, Sylverken AA, Larbi A, Sakyi SA, Asiedu SO. Molecular characterization of interactions between the D614G variant of SARS‐CoV‐2 S‐protein and neutralizing antibodies: A computational approach. Infect Genet Evol. 2021;91:104815. - PMC - PubMed

[4] Kwarteng A, Asiedu E, Sylverken AA, Larbi A, Sakyi SA, Asiedu SO. Molecular characterization of interactions between the D614G variant of SARS‐CoV‐2 S‐protein and neutralizing antibodies: A computational approach. Infect Genet Evol. 2021;91:104815. - PMC - PubMed

[5] Li Q, Wu J, Nie J, et al. The impact of mutations in SARS‐CoV‐2 spike on viral infectivity and antigenicity. Cell. 2020;182(5):1284‐1294.e1289. - PMC - PubMed

[6] Li Q, Wu J, Nie J, et al. The impact of mutations in SARS‐CoV‐2 spike on viral infectivity and antigenicity. Cell. 2020;182(5):1284‐1294.e1289. - PMC - PubMed

[7] Ke Z, Oton J, Qu K, et al. Structures and distributions of SARS‐CoV‐2 spike proteins on intact virions. Nature. 2020;588(7838):498‐502. - PMC - PubMed

[8] Ke Z, Oton J, Qu K, et al. Structures and distributions of SARS‐CoV‐2 spike proteins on intact virions. Nature. 2020;588(7838):498‐502. - PMC - PubMed

[9] Hodcroft EB, Domman DB, Snyder DJ, et al. Emergence in late 2020 of multiple lineages of SARS‐CoV‐2 Spike protein variants affecting amino acid position 677. medRxiv. 2021;2021. 10.1101/2021.02.12.21251658 - DOI

[10] Hodcroft EB, Domman DB, Snyder DJ, et al. Emergence in late 2020 of multiple lineages of SARS‐CoV‐2 Spike protein variants affecting amino acid position 677. medRxiv. 2021;2021. 10.1101/2021.02.12.21251658 - DOI

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N-terminal domain of SARS CoV-2 spike protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals

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N-terminal domain of SARS CoV-2 spike protein mutation associated reduction in effectivity of neutralizing antibody with vaccinated individuals

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Conflict of interest statement

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