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TitleNeutralizing antibodies protect mice against Venezuelan equine encephalitis virus aerosol challenge.
Journal, issue, pagesJ Exp Med, Vol. 219, Issue 4, Year 2022
Publish dateApr 4, 2022
AuthorsNatasha M Kafai / Lauren E Williamson / Elad Binshtein / Soila Sukupolvi-Petty / Christina L Gardner / Jaclyn Liu / Samantha Mackin / Arthur S Kim / Nurgun Kose / Robert H Carnahan / Ana Jung / Lindsay Droit / Douglas S Reed / Scott A Handley / William B Klimstra / James E Crowe / Michael S Diamond /
PubMed AbstractVenezuelan equine encephalitis virus (VEEV) remains a risk for epidemic emergence or use as an aerosolized bioweapon. To develop possible countermeasures, we isolated VEEV-specific neutralizing ...Venezuelan equine encephalitis virus (VEEV) remains a risk for epidemic emergence or use as an aerosolized bioweapon. To develop possible countermeasures, we isolated VEEV-specific neutralizing monoclonal antibodies (mAbs) from mice and a human immunized with attenuated VEEV strains. Functional assays and epitope mapping established that potently inhibitory anti-VEEV mAbs bind distinct antigenic sites in the A or B domains of the E2 glycoprotein and block multiple steps in the viral replication cycle including attachment, fusion, and egress. A 3.2-Å cryo-electron microscopy reconstruction of VEEV virus-like particles bound by a human Fab suggests that antibody engagement of the B domain may result in cross-linking of neighboring spikes to prevent conformational requirements for viral fusion. Prophylaxis or postexposure therapy with these mAbs protected mice against lethal aerosol challenge with VEEV. Our study defines functional and structural mechanisms of mAb protection and suggests that multiple antigenic determinants on VEEV can be targeted for vaccine or antibody-based therapeutic development.
External linksJ Exp Med / PubMed:35297953 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.2 Å
Structure data

25102

7sfu

EMDB-25102, PDB-7sfu:
CryoEM structure of Venezuelan Equine Encephalitis virus (VEEV) TC-83 strain VLP
Method: EM (single particle) / Resolution: 4.2 Å

25103

7sfv

EMDB-25103, PDB-7sfv:
CryoEM structure of Venezuelan Equine Encephalitis virus (VEEV) TC-83 strain VLP in complex with Fab hVEEV-63
Method: EM (single particle) / Resolution: 4.0 Å

25104

7sfw

EMDB-25104, PDB-7sfw:
CryoEM structure of Venezuelan Equine Encephalitis virus (VEEV) TC-83 strain VLP in complex with Fab hVEEV-63 (focus refine of the asymmetric unit)
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • venezuelan equine encephalitis virus (strain tc-83)
  • homo sapiens (human)
KeywordsVIRUS / VLP / VEEV / viral protein / VIRUS/IMMUNE SYSTEM / fab / VIRUS-IMMUNE SYSTEM complex

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