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TitleBroad neutralization of H1 and H3 viruses by adjuvanted influenza HA stem vaccines in nonhuman primates.
Journal, issue, pagesSci Transl Med, Vol. 13, Issue 583, Year 2021
Publish dateMar 3, 2021
AuthorsNicole Darricarrère / Yu Qiu / Masaru Kanekiyo / Adrian Creanga / Rebecca A Gillespie / Syed M Moin / Jacqueline Saleh / Jose Sancho / Te-Hui Chou / Yanfeng Zhou / Ruijun Zhang / Shujia Dai / Anthony Moody / Kevin O Saunders / Michelle C Crank / John R Mascola / Barney S Graham / Chih-Jen Wei / Gary J Nabel /
PubMed AbstractSeasonal influenza vaccines confer protection against specific viral strains but have restricted breadth that limits their protective efficacy. The H1 and H3 subtypes of influenza A virus cause most ...Seasonal influenza vaccines confer protection against specific viral strains but have restricted breadth that limits their protective efficacy. The H1 and H3 subtypes of influenza A virus cause most of the seasonal epidemics observed in humans and are the major drivers of influenza A virus-associated mortality. The consequences of pandemic spread of COVID-19 underscore the public health importance of prospective vaccine development. Here, we show that headless hemagglutinin (HA) stabilized-stem immunogens presented on ferritin nanoparticles elicit broadly neutralizing antibody (bnAb) responses to diverse H1 and H3 viruses in nonhuman primates (NHPs) when delivered with a squalene-based oil-in-water emulsion adjuvant, AF03. The neutralization potency and breadth of antibodies isolated from NHPs were comparable to human bnAbs and extended to mismatched heterosubtypic influenza viruses. Although NHPs lack the immunoglobulin germline VH1-69 residues associated with the most prevalent human stem-directed bnAbs, other gene families compensated to generate bnAbs. Isolation and structural analyses of vaccine-induced bnAbs revealed extensive interaction with the fusion peptide on the HA stem, which is essential for viral entry. Antibodies elicited by these headless HA stabilized-stem vaccines neutralized diverse H1 and H3 influenza viruses and shared a mode of recognition analogous to human bnAbs, suggesting that these vaccines have the potential to confer broadly protective immunity against diverse viruses responsible for seasonal and pandemic influenza infections in humans.
External linksSci Transl Med / PubMed:33658355
MethodsEM (single particle)
Resolution4.1 - 6.0 Å
Structure data

21973

6wzt

EMDB-21973, PDB-6wzt:
CryoEM structure of influenza hemagglutinin A/Victoria/361/2011 in complex with cyno antibody 3B10
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-22096:
CryoEM map of Full-length Influenza Hemagglutinin (A/Vietnam/1203/2004) in complex with 1C4 Fab Fragment
Method: EM (single particle) / Resolution: 6.0 Å

22180

6xgc

EMDB-22180, PDB-6xgc:
CryoEM structure of influenza hemagglutinin A/Michigan/45/2015 in complex with cyno antibody 1C4
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • influenza a virus
  • macaca fascicularis (crab-eating macaque)
  • influenza a virus (a/michigan/45/2015(h1n1))
KeywordsANTIVIRAL PROTEIN / influenza / hemagglutinin / antibody / vaccine / broadly neutralizing antibody

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