2021
DOI: 10.1016/j.nmni.2021.100889
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Extensive genetic diversity with novel mutations in spike glycoprotein of severe acute respiratory syndrome coronavirus 2, Bangladesh in late 2020

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Cited by 10 publications
(7 citation statements)
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“…The mutation was observed in the Delta For the first time, it was noted in variants isolated from India (156,157). This mutation was also reported in Bangladesh (179). The mutation augments infectivity and may help in the immune escape phenomena of the virus.…”
Section: P681rmentioning
confidence: 84%
“…The mutation was observed in the Delta For the first time, it was noted in variants isolated from India (156,157). This mutation was also reported in Bangladesh (179). The mutation augments infectivity and may help in the immune escape phenomena of the virus.…”
Section: P681rmentioning
confidence: 84%
“…Similarly, L452R mutation is reported in epsilon (B.1.427 and B.1.429), which is a variant of concern reported from California [17]. This mutation is reported to increase the rate of membrane fusion and thus lead to enhanced transmissibility [18]. The kappa variant thus epitomizes a conglomeration of key sequence variations that have previously been associated with important biological properties like enhanced viral attachment, cellular fusion and reduced neutralization with serum from convalescent individuals, vaccine recipients and monoclonal antibodies [19][20][21].…”
Section: Discussionmentioning
confidence: 89%
“…As these mutations are expected to destabilize the spike protein, they are expected to reduce antibody neutralization, which agrees with previous reports [ 24 , 27 ]. The mutation Q675H located in the Pre-Furin cleavage site in the spike protein, with the highest destabilizing ability, has appeared in Bangladesh in late 2020 [ 28 ]. However, some variants that have destabilized the protein with increased flexibility (e.g., E484K, K417 N, E484Q, Q675P, and Q675H) might impact the virus's ability to escape the antibodies neutralization by changing the antigenicity drift of the protein 3D structure; this is in agreement with a previous study [ [23] , [24] , [25] , [26] , [27] , [28] ].…”
Section: Discussionmentioning
confidence: 99%