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Unique structural solution from a V H 3-30 antibody targeting the hemagglutinin stem of influenza A viruses
- Source :
- Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
- Publication Year :
- 2021
- Publisher :
- Nature Portfolio, 2021.
-
Abstract
- Broadly neutralizing antibodies (bnAbs) targeting conserved influenza A virus (IAV) hemagglutinin (HA) epitopes can provide valuable information for accelerating universal vaccine designs. Here, we report structural details for heterosubtypic recognition of HA from circulating and emerging IAVs by the human antibody 3I14. Somatic hypermutations play a critical role in shaping the HCDR3, which alone and uniquely among VH3-30 derived antibodies, forms contacts with five sub-pockets within the HA-stem hydrophobic groove. 3I14 light-chain interactions are also key for binding HA and contribute a large buried surface area spanning two HA protomers. Comparison of 3I14 to bnAbs from several defined classes provide insights to the bias selection of VH3-30 antibodies and reveals that 3I14 represents a novel structural solution within the VH3-30 repertoire. The structures reported here improve our understanding of cross-group heterosubtypic binding activity, providing the basis for advancing immunogen designs aimed at eliciting a broadly protective response to IAV.
- Subjects :
- 0301 basic medicine
Multidisciplinary
Immunogen
biology
Repertoire
Science
General Physics and Astronomy
Hemagglutinin (influenza)
Influenza a
General Chemistry
Computational biology
medicine.disease_cause
General Biochemistry, Genetics and Molecular Biology
Epitope
03 medical and health sciences
030104 developmental biology
0302 clinical medicine
Antibody targeting
biology.protein
Influenza A virus
medicine
Antibody
030217 neurology & neurosurgery
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Volume :
- 12
- Issue :
- 1
- Database :
- OpenAIRE
- Journal :
- Nature Communications
- Accession number :
- edsair.doi.dedup.....7cb5870d6b18ca88328d76443f6014d5