Structural basis for the divergent evolution of influenza B virus hemagglutinin

Ni, Fengyun; Kondrashkina, Elena; Wang, Qinghua

doi:10.1016/j.virol.2013.07.035

Cited by 51 publications

(71 citation statements)

References 53 publications

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“…In total, 22,000 particles were manually picked from 130 CCD images and extracted using a 160px box size with the e2boxer.py software included into EMAN2 distribution48 and subjected to reference free 2D classification with the software suite Relion49. In total, 22,000 particles were used to determine a 3D reconstruction of FluB HA bound to 46B8 Fab in Relion, using as a starting model the crystal structure of the B/Yamanashi/166/1998 HA (PDB ID 4M40) low pass filtered to a resolution of 60 Å50. This HA crystal structure and a homology model for the 46B8 Fab based on homologous antibody crystal structures and generated using the programme MOE (Chemical Computing Group) were fitted into the EM density using the fit in map algorithm in Chimera51.…”

Section: Methodsmentioning

confidence: 99%

A broadly protective therapeutic antibody against influenza B virus with two mechanisms of action

Chai¹,

Swem²,

Park³

et al. 2017

Nat Commun

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Influenza B virus (IBV) causes annual influenza epidemics around the world. Here we use an in vivo plasmablast enrichment technique to isolate a human monoclonal antibody, 46B8 that neutralizes all IBVs tested in vitro and protects mice against lethal challenge of all IBVs tested when administered 72 h post infection. 46B8 demonstrates a superior therapeutic benefit over Tamiflu and has an additive antiviral effect in combination with Tamiflu. 46B8 binds to a conserved epitope in the vestigial esterase domain of hemagglutinin (HA) and blocks HA-mediated membrane fusion. After passage of the B/Brisbane/60/2008 virus in the presence of 46B8, we isolated three resistant clones, all harbouring the same mutation (Ser301Phe) in HA that abolishes 46B8 binding to HA at low pH. Interestingly, 46B8 is still able to protect mice against lethal challenge of the mutant viruses, possibly owing to its ability to mediate antibody-dependent cellular cytotoxicity (ADCC).

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Section: Methodsmentioning

confidence: 99%

A broadly protective therapeutic antibody against influenza B virus with two mechanisms of action

Chai¹,

Swem²,

Park³

et al. 2017

Nat Commun

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“…A wealth of structures of influenza A virus HA subtypes H1–H3, H5, H7, H9, H13, H14, and H17 17 and influenza B virus HA 22,26,27 in the prefusion state and of influenza A/H3N2 HA in the postfusion state 15,18 exist. The newly determined structure of influenza B virus HA 2 in the postfusion state as reported here has filled an important structural gap in the field and allowed the identification of conserved features in the conformational changes of both influenza A and B virus HA.…”

Section: Discussionmentioning

confidence: 99%

Structural Insights into the Membrane Fusion Mechanism Mediated by Influenza Virus Hemagglutinin

Chen

Shen

et al. 2014

Biochemistry

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Membrane fusion is involved in many fundamental cellular processes and entry of enveloped viruses into host cells. Influenza type A virus HA has long served as a paradigm for mechanistic studies of protein-mediated membrane fusion via large-scale structural rearrangements induced by acidic pH. Here we report the newly determined crystal structure of influenza B virus HA2 in the postfusion state. Together with a large number of previously determined prefusion structures of influenza A and B virus HA and a postfusion structure of influenza A/H3N2 HA2, we identified conserved features that are shared between influenza A and B virus HA in the conformational transition and documented substantial differences that likely influence the detailed mechanisms of this process. Further studies are needed to dissect the effects of these and other structural differences in HA conformational changes and influenza pathogenicity and transmission, which may ultimately expedite the discovery of novel anti-influenza fusion inhibitors.

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“…The structures are visualized with JSmol (37). For H3N2, we use structure 5HMG (38); for H1N1pdm, we use 4LXV (39); and, for the influenza B Victoria and Yamagata lineages, we use 4FQM (40) and 4M40 (41). The structure visualization is available at hi.nextflu.org/H3N2/3y/.…”

Section: Methodsmentioning

confidence: 99%

Prediction, dynamics, and visualization of antigenic phenotypes of seasonal influenza viruses

Neher

Bedford

Daniels

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

197

270

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Human seasonal influenza viruses evolve rapidly, enabling the virus population to evade immunity and reinfect previously infected individuals. Antigenic properties are largely determined by the surface glycoprotein hemagglutinin (HA), and amino acid substitutions at exposed epitope sites in HA mediate loss of recognition by antibodies. Here, we show that antigenic differences measured through serological assay data are well described by a sum of antigenic changes along the path connecting viruses in a phylogenetic tree. This mapping onto the tree allows prediction of antigenicity from HA sequence data alone. The mapping can further be used to make predictions about the makeup of the future A(H3N2) seasonal influenza virus population, and we compare predictions between models with serological and sequence data. To make timely model output readily available, we developed a web browserbased application that visualizes antigenic data on a continuously updated phylogeny.evolution | antigenic distance | phylogenetic tree

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Structural basis for the divergent evolution of influenza B virus hemagglutinin

Cited by 51 publications

References 53 publications

A broadly protective therapeutic antibody against influenza B virus with two mechanisms of action

A broadly protective therapeutic antibody against influenza B virus with two mechanisms of action

Structural Insights into the Membrane Fusion Mechanism Mediated by Influenza Virus Hemagglutinin

Prediction, dynamics, and visualization of antigenic phenotypes of seasonal influenza viruses

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