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Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion pept...

Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion pept...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e636e8ff307e4e158f7f9667c39522e1

Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

About this item

Full title

Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2023-11, Vol.14 (1), p.7593-17, Article 7593

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The HIV-1 fusion peptide (FP) represents a promising vaccine target, but global FP sequence diversity among circulating strains has limited anti-FP antibodies to ~60% neutralization breadth. Here we evolve the FP-targeting antibody VRC34.01 in vitro to enhance FP-neutralization using site saturation mutagenesis and yeast display. Successive rounds...

Alternative Titles

Full title

Antibody-directed evolution reveals a mechanism for enhanced neutralization at the HIV-1 fusion peptide site

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_e636e8ff307e4e158f7f9667c39522e1

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_e636e8ff307e4e158f7f9667c39522e1

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-023-42098-5

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