Viral membrane fusion

By S. Harrison. Nature Structural &Molecular Biology, 2008

1,392 citations recorded by the source corpus.

Infection by viruses having lipid-bilayer envelopes proceeds through fusion of the viral membrane with a membrane of the target cell. Viral 'fusion proteins' facilitate this process. They vary greatly in structure, but all seem to have a common mechanism of action, in which a ligand-triggered, large-scale conformational change in the fusion protein is coupled to apposition and merger of the two bilayers. We describe three examples—the influenza virus hemagglutinin, the flavivirus E protein and the vesicular stomatitis virus G protein—in some detail, to illustrate the ways in which different structures have evolved to implement this common mechanism. Fusion inhibitors can be effective antiviral agents.

Subfields: Cardiology and Cardiovascular Medicine, Epidemiology, Immunology

View Paper: https://www.semanticscholar.org/paper/c8d74ed230c0498a5dcfe07783a0767fbe0e0ce5

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In Cardiology and Cardiovascular Medicine

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In Immunology

Citations in the corpus

Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites (2009, background): “E viruses access their host cells by a process of membrane fusion that is mediated by a specific fusion, or ‘‘spike’’ protein, encoded by the virus and embedded in the viral envelope (1, 2).”
New Vaccine Design and Delivery Technologies (2019, background): “For example, many viral glycoproteins that [25] .”
Evolutionary velocity with protein language models (2021, positive): “We next analyzed the evolution of inﬂuenza A hemagglutinin (HA), a more variable protein on the viral surface responsible for viral-host membrane fusion (Eckert and Kim, 2001; Harrison, 2008).”
Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy (2016, background): “Comparison of the prefusion HCoV-NL63 S 2 subunit with the structure of the postfusion core suggests that the C-terminal region of the connector domain and the stem helix must refold and/or change conformation to yield the canonical 'trimer of hairpin' conformation that mediates fusion of the host a”
Distinct Patterns of IFITM-Mediated Restriction of Filoviruses, SARS Coronavirus, and Influenza A Virus (2011, background): “engagement, these entry proteins undergo conformational changes that ultimately promote mixing of viral and cellular membrane lipids, formation of a fusion pore, and transfer of the viral genome to the cell cytoplasm [6].”
Molecular machines governing exocytosis of synaptic vesicles (2012, background): “This helps to explain why unrelated classes of fusion proteins evolved in parallel to the SNAREs, such as those fusing cells (95), viruses (96), mitochondria (97) or the endoplasmic reticulum (98).”
Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains (2017, neutral): “The spatial organizations of MERS-CoV and SARS-CoV S proteins resemble that of inﬂuenza virus hemagglutinin (HA) protein, which also has two cleaved subunits (HA1 and HA2) and the HA1 subunit must dissociate from HA2 before activation of membrane fusion under low pH environment in the endosome 21 .”
Structural insights into coronavirus entry (2019, background): “The free energy released upon S2 refolding from the prefusion to the postfusion state is believed to bring the viral and host mem- branes in close proximity and promote membrane merger (Harrison, 2008).”
Viral membrane fusion (2015, background): “Viral fusion proteins fall into a small number of structural classes -- three reasonably well characterized ones at the time of this review[7].”
Structural Characterization of the glycoprotein GP2 Core Domain from the CAS Virus, a Novel Arenavirus-like Species (2013, background): “The “class I” viral fusion proteins, which include those of the human immunodeficiency viruses, influenza, Ebola viruses [exemplified by Ebola virus (EBOV) and Sudan virus (SUDV)] and Marburg virus (MARV), are defined by the formation of a core, trimeric α-helical bundle by the ectodomain of the tra”