Unknown

Dataset Information

0

Viral membrane fusion.


ABSTRACT: 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.

SUBMITTER: Harrison SC 

PROVIDER: S-EPMC4424100 | biostudies-literature | 2015 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Viral membrane fusion.

Harrison Stephen C SC  

Virology 20150410


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 und  ...[more]

Similar Datasets

| S-EPMC7412173 | biostudies-literature
| S-EPMC7080115 | biostudies-literature
| S-EPMC5783950 | biostudies-literature
| S-EPMC6398481 | biostudies-literature
| S-EPMC7094410 | biostudies-literature
| S-EPMC4945621 | biostudies-literature
| S-EPMC8709411 | biostudies-literature
| S-EPMC4728575 | biostudies-literature