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TitleStructure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 110, Issue 12, Page 4592-4597, Year 2013
Publish dateMar 19, 2013
AuthorsAudray K Harris / Joel R Meyerson / Yumiko Matsuoka / Oleg Kuybeda / Amy Moran / Donald Bliss / Suman R Das / Jonathan W Yewdell / Guillermo Sapiro / Kanta Subbarao / Sriram Subramaniam /
PubMed AbstractRapid antigenic variation of HA, the major virion surface protein of influenza A virus, remains the principal challenge to the development of broader and more effective vaccines. Some regions of HA, ...Rapid antigenic variation of HA, the major virion surface protein of influenza A virus, remains the principal challenge to the development of broader and more effective vaccines. Some regions of HA, such as the stem region proximal to the viral membrane, are nevertheless highly conserved across strains and among most subtypes. A fundamental question in vaccine design is the extent to which HA stem regions on the surface of the virus are accessible to broadly neutralizing antibodies. Here we report 3D structures derived from cryoelectron tomography of HA on intact 2009 H1N1 pandemic virions in the presence and absence of the antibody C179, which neutralizes viruses expressing a broad range of HA subtypes, including H1, H2, H5, H6, and H9. By fitting previously derived crystallographic structures of trimeric HA into the density maps, we deduced the locations of the molecular surfaces of HA involved in interaction with C179. Using computational methods to distinguish individual unliganded HA trimers from those that have bound C179 antibody, we demonstrate that ∼75% of HA trimers on the surface of the virus have C179 bound to the stem domain. Thus, despite their close packing on the viral membrane, the majority of HA trimers on intact virions are available to bind anti-stem antibodies that target conserved HA epitopes, establishing the feasibility of universal influenza vaccines that elicit such antibodies.
External linksProc Natl Acad Sci U S A / PubMed:23460696 / PubMed Central
MethodsEM (subtomogram averaging)
Structure data

EMDB-5682:
Molecular structure of the native influenza hemagglutinin H1 on virions
Method: EM (subtomogram averaging)

EMDB-5683:
Molecular structure of the native influenza hemagglutinin H1 on virions
Method: EM (subtomogram averaging)

EMDB-5684:
Molecular structure of the native influenza hemagglutinin H1 on virions complexed with broadly neutralizing stem antibody C179
Method: EM (subtomogram averaging)

EMDB-5685:
Molecular structure of the native influenza hemagglutinin H1 on virions complexed with broadly neutralizing stem antibody C179
Method: EM (subtomogram averaging)

EMDB-5686:
Molecular structure of the native influenza hemagglutinin H3 on virions
Method: EM (subtomogram averaging)

EMDB-5687:
Molecular structure of the native influenza hemagglutinin H3 on virions
Method: EM (subtomogram averaging)

Source
  • Influenza A virus (A/California/07/2009(H1N1))
  • Influenza A virus (A/Aichi/2/1968(H3N2))

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