SARS-CoV-2 spike protein mutations: Difference between revisions
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:1. <scene name='87/870593/Spike_open/2'>N501Y: Asn at sequence position 501 mutated to Tyr.</scene> (See [[Amino Acids|3- and 1-letter amino acid abbreviations]].) This mutation is in the receptor-binding domain of spike protein, and '''increases binding affinity''' for [[Angiotensin-Converting Enzyme|ACE-2]], the receptor that SARS-CoV-2 uses to enter and infect cells<ref name="starr">PMID: 32841599</ref><ref name="teruel">[https://www.biorxiv.org/content/10.1101/2020.12.16.423118v1 Modelling conformational state dynamics and its role on infection for SARS-CoV-2 Spike protein variants], preprint posted December 17, 2020 by Teruel, Maihot & Najmanovich. Computational work suggests that N501Y increases the occupancy of the open (primed) state of the spike protein.</ref><ref name="zahradnik">[https://www.biorxiv.org/content/10.1101/2021.01.06.425392v1 SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor] by Jiri Zahradnik ''et al.'', preprint posted January 6, 2020.</ref>. | :1. <scene name='87/870593/Spike_open/2'>N501Y: Asn at sequence position 501 mutated to Tyr.</scene> (See [[Amino Acids|3- and 1-letter amino acid abbreviations]].) This mutation is in the receptor-binding domain of spike protein, and '''increases binding affinity''' for [[Angiotensin-Converting Enzyme|ACE-2]], the receptor that SARS-CoV-2 uses to enter and infect cells<ref name="starr">PMID: 32841599</ref><ref name="teruel">[https://www.biorxiv.org/content/10.1101/2020.12.16.423118v1 Modelling conformational state dynamics and its role on infection for SARS-CoV-2 Spike protein variants], preprint posted December 17, 2020 by Teruel, Maihot & Najmanovich. Computational work suggests that N501Y increases the occupancy of the open (primed) state of the spike protein.</ref><ref name="zahradnik">[https://www.biorxiv.org/content/10.1101/2021.01.06.425392v1 SARS-CoV-2 RBD in vitro evolution follows contagious mutation spread, yet generates an able infection inhibitor] by Jiri Zahradnik ''et al.'', preprint posted January 6, 2020.</ref>. | ||
:2 & 3: <scene name='87/870593/Spike_open/3'>Deletion of His 69 and Val 70</scene>. These deletions are in a position likely to affect the ability of certain antibodies to block infection. However, since vaccination induces antibodies to many parts of the spike protein, these mutations alone are unlikely to reduce the effectiveness of the current vaccines (see below). | :2 & 3: <scene name='87/870593/Spike_open/3'>Deletion of His 69 and Val 70</scene>. These deletions are in a position likely to affect the ability of certain antibodies to block infection. However, since vaccination induces antibodies to many parts of the spike protein, these mutations alone are unlikely to reduce the effectiveness of the current vaccines (see below). These deletions have been useful in epidemiologic screening for B.1.1.7 without needing to sequence all samples<ref name="embl1">[https://www.embl.org/news/science/sars-cov-2-b117/ The SARS-CoV-2 B.1.1.7 lineage: Summary of evidence from the U.K.] by Moritz Gerstung of EMBL-EBI ''et al.'', January 20, 2021.</ref>. | ||
:4. <scene name='87/870593/Spike_open/5'>P681H: Pro 681 to His</scene>. This mutation is in the [[SARS-CoV-2 spike protein priming by furin|furin cleavage site that primes spike protein]]. The effects of this mutation are not yet known. | :4. <scene name='87/870593/Spike_open/5'>P681H: Pro 681 to His</scene>. This mutation is in the [[SARS-CoV-2 spike protein priming by furin|furin cleavage site that primes spike protein]]. The effects of this mutation are not yet known. | ||