Journal
TRAFFIC
Volume 17, Issue 6, Pages 593-614Publisher
WILEY
DOI: 10.1111/tra.12389
Keywords
enveloped virus; fuse; low pH; membrane; prime; proteases; trigger; viral fusion protein; virus entry; virus receptors
Categories
Funding
- National Institutes of Health [R21 AI103601, RO1 AI114776, R21 AI111085, R21 AI117300]
- National Science Foundation [1504846]
- National Institute of Allergy and Infectious Diseases, National Institutes of Health, Department of Health and Human Services, under CEIRS [HHSN272201400005C]
- Cornell Feline Health Center
- Winn Feline Health Foundation
- Morris Animal Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [1504846] Funding Source: National Science Foundation
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Ari Helenius launched the field of enveloped virus fusion in endosomes with a seminal paper in the Journal of Cell Biology in 1980. In the intervening years, a great deal has been learned about the structures and mechanisms of viral membrane fusion proteins as well as about the endosomes in which different enveloped viruses fuse and the endosomal cues that trigger fusion. We now recognize three classes of viral membrane fusion proteins based on structural criteria and four mechanisms of fusion triggering. After reviewing general features of viral membrane fusion proteins and viral fusion in endosomes, we delve into three characterized mechanisms for viral fusion triggering in endosomes: by low pH, by receptor binding plus low pH and by receptor binding plus the action of a protease. We end with a discussion of viruses that may employ novel endosomal fusion-triggering mechanisms. A key take-home message is that enveloped viruses that enter cells by fusing in endosomes traverse the endocytic pathway until they reach an endosome that has all of the environmental conditions (pH, proteases, ions, intracellular receptors and lipid composition) to (if needed) prime and (in all cases) trigger the fusion protein and to support membrane fusion.
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