Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies. Issue 12 (8th November 2021)

• Record Type: Journal Article
• Authors: Lousa, Diana; Soares, Cláudio M.
• Is Part Of: FEBS open bio. Volume 11:Issue 12(2021)
• Page Start: 3253
• Page End: 3261
• Publication Date: 2021-11-08
• Subjects: biophysical assays -- hemagglutinin -- influenza -- membrane fusion -- molecular dynamics simulation -- virus; Molecular biology -- Periodicals; Cytology -- Periodicals; Life sciences -- Periodicals; Biological Science Disciplines -- Periodicals; Molecular Biology -- Periodicals; Cell Biology -- Periodicals; Cytology; Life sciences; Molecular biology; Periodicals; 572.805
• DOI: 10.1002/2211-5463.13323
• Languages: English
• ISSNs: 2211-5463

Abstract

Abstract : A key step in infections by enveloped viruses, such as influenza, is the fusion between the viral envelope and the host cell membrane, which allows the virus to insert its genetic material into the host cell and replicate. The influenza virus fusion process is promoted by hemagglutinin (HA), a glycoprotein that contains three identical monomers composed of two polypeptide chains (HA1 and HA2). Early studies on this protein revealed that HA‐mediated fusion involves the insertion of the HA2 N‐terminal segment into the host membrane and that this segment, known as the fusion peptide, is a key player in the fusion process. This mini‐review highlights the main findings that have been obtained by experimental and computational studies on the HA fusion peptide, which give us a glimpse of its mode of action. Abstract : A key step in influenza infection is the fusion of the viral and host membranes, promoted by the protein hemagglutinin, which contains a fusion peptide that inserts and destabilizes the host membrane. This review highlights the major findings of experimental and computational studies, which analyzed the properties of this peptide, including the role of key residues for its fusogenic activity.