Viral membrane fusion

By S. Harrison. 2015

504 citations recorded by the source corpus.

Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a “fusion loop” or “fusion peptide”) engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics.

Subfields: Animal Science and Zoology, Ecology, Genetics

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In Animal Science and Zoology

1. D. Veesler

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1. David Baker
2. Neil P. King
3. William F. DeGrado
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Citations in the corpus

• Induction of Potent Neutralizing Antibody Responses by a Designed Protein Nanoparticle Vaccine for Respiratory Syncytial Virus (2019, background): “F is a trimeric type I fusion glycoprotein responsible for merging the viral membrane with cellular membranes, and, like many other viral fusion glycoproteins, it undergoes major structural rearrangements as it transitions from the prefusion to the postfusion state (Harrison, 2015).”
• Elicitation of broadly protective immunity to influenza by multivalent hemagglutinin nanoparticle vaccines (2020, background): “HA is a homotrimeric class I fusion protein, consisting of a head domain that facilitates host cell attachment by binding cell-surface sialosides and a stem domain containing the membrane fusion machinery 18,19 ​ .”
• The human coronavirus HCoV-229E S-protein structure and receptor binding (2019, background): “The coronavirus S2 418 subunit is large and the conformational changes on conversion to the post-fusion are more 419 extensive than that shown by many other viral fusion proteins (42, 43).”