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- PDB-7x6o: Cryo-EM structure of H1 hemagglutinin from A/Washington/05/2011 i... -

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Basic information

Entry
Database: PDB / ID: 7x6o
TitleCryo-EM structure of H1 hemagglutinin from A/Washington/05/2011 in complex with a neutralizing antibody 28-12
Components
  • (Hemagglutinin) x 2
  • Heavy chain of antibody 12 fab
  • The light chain of antibody 12 fab
KeywordsVIRAL PROTEIN / Influenza A virus / H1N1 / antibody 12 fab / cryo-EM
Function / homology
Function and homology information


viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane
Similarity search - Function
Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein
Similarity search - Domain/homology
Hemagglutinin / Hemagglutinin
Similarity search - Component
Biological speciesInfluenza A virus
Homo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsCong, Y. / Liu, C.X.
Funding support China, 1items
OrganizationGrant numberCountry
Chinese Academy of SciencesXDB29040300 China
CitationJournal: Nat Commun / Year: 2022
Title: Unique binding pattern for a lineage of human antibodies with broad reactivity against influenza A virus.
Authors: Xiaoyu Sun / Caixuan Liu / Xiao Lu / Zhiyang Ling / Chunyan Yi / Zhen Zhang / Zi Li / Mingliang Jin / Wenshuai Wang / Shubing Tang / Fangfang Wang / Fang Wang / Sonam Wangmo / Shuangfeng ...Authors: Xiaoyu Sun / Caixuan Liu / Xiao Lu / Zhiyang Ling / Chunyan Yi / Zhen Zhang / Zi Li / Mingliang Jin / Wenshuai Wang / Shubing Tang / Fangfang Wang / Fang Wang / Sonam Wangmo / Shuangfeng Chen / Li Li / Liyan Ma / Yaguang Zhang / Zhuo Yang / Xiaoping Dong / Zhikang Qian / Jianping Ding / Dayan Wang / Yao Cong / Bing Sun /
Abstract: Most structurally characterized broadly neutralizing antibodies (bnAbs) against influenza A viruses (IAVs) target the conserved conformational epitopes of hemagglutinin (HA). Here, we report a ...Most structurally characterized broadly neutralizing antibodies (bnAbs) against influenza A viruses (IAVs) target the conserved conformational epitopes of hemagglutinin (HA). Here, we report a lineage of naturally occurring human antibodies sharing the same germline gene, V3-48/V1-12. These antibodies broadly neutralize the major circulating strains of IAV in vitro and in vivo mainly by binding a contiguous epitope of H3N2 HA, but a conformational epitope of H1N1 HA, respectively. Our structural and functional studies of antibody 28-12 revealed that the continuous amino acids in helix A, particularly N49 of H3 HA, are critical to determine the binding feature with 28-12. In contrast, the conformational epitope feature is dependent on the discontinuous segments involving helix A, the fusion peptide, and several HA1 residues within H1N1 HA. We report that this antibody was initially selected by H3 (group 2) viruses and evolved via somatic hypermutation to enhance the reactivity to H3 and acquire cross-neutralization to H1 (group 1) virus. These findings enrich our understanding of different antigenic determinants of heterosubtypic influenza viruses for the recognition of bnAbs and provide a reference for the design of influenza vaccines and more effective antiviral drugs.
History
DepositionMar 7, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 23, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 30, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / em_admin / pdbx_entry_details / pdbx_modification_feature
Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hemagglutinin
B: Hemagglutinin
C: Heavy chain of antibody 12 fab
D: The light chain of antibody 12 fab
E: Hemagglutinin
G: Hemagglutinin
I: Heavy chain of antibody 12 fab
K: The light chain of antibody 12 fab
F: Hemagglutinin
H: Hemagglutinin
J: Heavy chain of antibody 12 fab
L: The light chain of antibody 12 fab


Theoretical massNumber of molelcules
Total (without water)314,84212
Polymers314,84212
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Hemagglutinin


Mass: 37055.742 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Gene: HA / Production host: Insecta environmental sample (insect) / References: UniProt: A0A2R4G8F1
#2: Protein Hemagglutinin


Mass: 20160.332 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Freiburg/728006/2011(H1N1) / Gene: HA / Production host: Insecta environmental sample (insect) / References: UniProt: J7GXV4
#3: Antibody Heavy chain of antibody 12 fab


Mass: 24466.277 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)
#4: Antibody The light chain of antibody 12 fab


Mass: 23264.861 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Insecta environmental sample (insect)
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: H1 hemagglutinin from A/Washington/05/2011 in complex with a neutralizing antibody 28-12
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Influenza A virus
Source (recombinant)Organism: Insecta environmental sample (insect)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 3000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 38 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 124947 / Symmetry type: POINT

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