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Basic Characteristics of Mutations
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Mutation Site
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S13I |
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Mutation Site Sentence
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A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429); which was originally detected in California; carries spike glycoprotein mutations S13I in the signal peptide; W152C in the N-terminal domain (NTD); and L452R in the receptor-binding domain (RBD). |
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Mutation Level
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Amino acid level |
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Mutation Type
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Nonsynonymous substitution |
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Gene/Protein/Region
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S |
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Standardized Encoding Gene
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S
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Genotype/Subtype
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CAL.20C |
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Viral Reference
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-
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Functional Impact and Mechanisms
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Disease
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COVID-19
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Immune
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- |
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Target Gene
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-
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Clinical and Epidemiological Correlations
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Clinical Information
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- |
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Treatment
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- |
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Location
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- |
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Literature Information
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PMID
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34210893
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Title
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SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern
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Author
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McCallum M,Bassi J,De Marco A,Chen A,Walls AC,Di Iulio J,Tortorici MA,Navarro MJ,Silacci-Fregni C,Saliba C,Sprouse KR,Agostini M,Pinto D,Culap K,Bianchi S,Jaconi S,Cameroni E,Bowen JE,Tilles SW,Pizzuto MS,Guastalla SB,Bona G,Pellanda AF,Garzoni C,Van Voorhis WC,Rosen LE,Snell G,Telenti A,Virgin HW,Piccoli L,Corti D,Veesler D
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Journal
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Science (New York, N.Y.)
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Journal Info
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2021 Aug 6;373(6555):648-654
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Abstract
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A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429), which was originally detected in California, carries spike glycoprotein mutations S13I in the signal peptide, W152C in the N-terminal domain (NTD), and L452R in the receptor-binding domain (RBD). Plasma from individuals vaccinated with a Wuhan-1 isolate-based messenger RNA vaccine or from convalescent individuals exhibited neutralizing titers that were reduced 2- to 3.5-fold against the B.1.427/B.1.429 variant relative to wild-type pseudoviruses. The L452R mutation reduced neutralizing activity in 14 of 34 RBD-specific monoclonal antibodies (mAbs). The S13I and W152C mutations resulted in total loss of neutralization for 10 of 10 NTD-specific mAbs because the NTD antigenic supersite was remodeled by a shift of the signal peptide cleavage site and the formation of a new disulfide bond, as revealed by mass spectrometry and structural studies.
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Sequence Data
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-
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