Structural insights into the design of novel anti-influenza therapies
Identifieur interne : 000154 ( Main/Curation ); précédent : 000153; suivant : 000155Structural insights into the design of novel anti-influenza therapies
Auteurs : Nicholas C. Wu [États-Unis] ; Ian A. Wilson [États-Unis]Source :
- Nature structural & molecular biology [ 1545-9993 ] ; 2018.
Abstract
A limited arsenal of therapies is available to tackle the emergence of a future influenza pandemic or even to effectively deal with the continual outbreaks of seasonal influenza. However, recent findings hold great promise for design of novel vaccines and therapeutics, including the possibility of more universal treatments. A major contribution to those advances comes from structural biology, in particular from the many studies on influenza hemagglutinin (HA), the major surface antigen. The HA primary function is to enable the virus to enter host cells, and structural work has revealed the various HA conformational forms generated during the entry process. Other studies have explored how human broadly neutralizing antibodies (bnAbs), designed proteins, peptides and small molecules, can inhibit and neutralize the virus. Here we review milestones in HA structural biology and how the recent insights from broadly neutralizing antibodies are leading to design of novel vaccines and therapeutics.
Url:
DOI: 10.1038/s41594-018-0025-9
PubMed: 29396418
PubMed Central: 5930012
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<front><div type="abstract" xml:lang="en"><p id="P1">A limited arsenal of therapies is available to tackle the emergence of a future influenza pandemic or even to effectively deal with the continual outbreaks of seasonal influenza. However, recent findings hold great promise for design of novel vaccines and therapeutics, including the possibility of more universal treatments. A major contribution to those advances comes from structural biology, in particular from the many studies on influenza hemagglutinin (HA), the major surface antigen. The HA primary function is to enable the virus to enter host cells, and structural work has revealed the various HA conformational forms generated during the entry process. Other studies have explored how human broadly neutralizing antibodies (bnAbs), designed proteins, peptides and small molecules, can inhibit and neutralize the virus. Here we review milestones in HA structural biology and how the recent insights from broadly neutralizing antibodies are leading to design of novel vaccines and therapeutics.</p>
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