The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Fusion of Enveloped Viruses in Endosomes
Open accessAbstract
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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Citations
Cites
Structure of influenza haemagglutinin at the pH of membrane fusion
Bullough, P. A., Hughson, F. M., Skehel, J. J., & Wiley, D. C. (1994) · Nature · doi:10.1038/371037a0 · Cited by 1,564
Imai, M., Watanabe, T., Hatta, M., Das, S. C., Ozawa, M., Shinya, K., Zhong, G., Hanson, A., Katsura, H., Watanabe, S., et al. (2012) · Nature · doi:10.1038/nature10831 · Cited by 1,523
Mercer, J., Schelhaas, M., & Helenius, A. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060208-104626 · Cited by 1,057
Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme
White, J. M., Delos, S. E., Brecher, M., & Schornberg, K. (2008) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230802058320 · Cited by 892
Self-citationPre-fusion structure of a human coronavirus spike protein
Kirchdoerfer, R. N., Cottrell, C. A., Wang, N., Pallesen, J., Yassine, H. M., Turner, H. L., Corbett, K. S., Graham, B. S., McLellan, J. S., & Ward, A. B. (2016) · Nature · doi:10.1038/nature17200 · Cited by 765
Skehel, J. J., Bayley, P. M., Brown, E. B., Martin, S. R., Waterfield, M. D., White, J. M., Wilson, I. A., & Wiley, D. C. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.4.968 · Cited by 726
Self-citationWilen, C. B., Tilton, J. C., & Doms, R. W. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006866 · Cited by 654
Cited by
Drug Combinations as a First Line of Defense against Coronaviruses and Other Emerging Viruses
White, J. M., Schiffer, J. T., Bender Ignacio, R. A., Xu, S., Kainov, D., Ianevski, A., Aittokallio, T., Frieman, M., Olinger, G. G., & Polyak, S. J. (2021) · mBio · doi:10.1128/mbio.03347-21 · Cited by 64
Self-citationFernández, I., Dynesen, L. T., Coquin, Y., Pederzoli, R., Brun, D., Haouz, A., Gessain, A., Rey, F. A., Buseyne, F., & Backovic, M. (2023) · Nature Communications · doi:10.1038/s41467-023-36923-0 · Cited by 11
Metadata
- Authors
- White, J. M., & Whittaker, G. R.
- Venue
- Traffic
- Publisher
- Wiley
- Published
- 2016-04-07
- Volume
- 17
- Issue
- 6
- Pages
- 593-614
- ISSN
- 1398-9219 (ISSN-L)
- 1600-0854
- OpenAlex
- W2288648350
- Cited by
- 397
- References
- 7
- FWCI
- 17.99
- Type
- journal article
- Language
- en
- Open access
- green
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