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Article

Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies.

Structure (London, England : 1993) - 1 Jul 2021

Cerutti Gabriele, Rapp Micah, Guo Yicheng, Bahna Fabiana, Bimela Jude, Reddem Eswar R, Yu Jian, Wang Pengfei, Liu Lihong, Huang Yaoxing, Ho David D, Kwong Peter D, Sheng Zizhang, Shapiro Lawrence

Abstract excerpt

Emerging SARS-CoV-2 strains, B.1.1.7 and B.1.351, from the UK and South Africa, respectively, show decreased neutralization by monoclonal antibodies and convalescent or vaccinee sera raised against the original wild-type virus, and are thus of clinical concern. However, the neutralization potency of two antibodies, 1-57 and 2-7, which target the receptor-binding domain (RBD) of the spike, was unaffected by these...

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Share to Angiotensin-Converting Enzyme 2
Share to Antibodies, Neutralizing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Conformation, alpha-Helical

Share to Protein Conformation, beta-Strand

Share to Protein Interaction Domains and Motifs

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Identifiers

PMID: 34111408
DOI: 10.1016/j.str.2021.05.014
PMCID: PMC8188728

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026.

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