The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Influenza hemagglutinin is spring-loaded by a metastable native conformation
Open accessAbstract
Enveloped viruses enter cells by protein-mediated membrane fusion. For influenza virus, membrane fusion is regulated by the conformational state of the hemagglutinin (HA) protein, which switches from a native (nonfusogenic) structure to a fusion-active (fusogenic) conformation when exposed to the acidic environment of the cellular endosome. Here we demonstrate that destabilization of HA at neutral pH, with either heat or the denaturant urea, triggers a conformational change that is biochemically indistinguishable from the change triggered by low pH. In each case, the conformational change is coincident with induction of membrane-fusion activity, providing strong evidence that the fusogenic structure is formed. These results indicate that the native structure of HA is trapped in a metastable state and that the fusogenic conformation is released by destabilization of native structure. This strategy may be shared by other enveloped viruses, including those that enter the cell at neutral pH, and could have implications for understanding the membrane-fusion step of HIV infection.
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Cited by
Receptor Binding and Membrane Fusion in Virus Entry: The Influenza Hemagglutinin
Skehel, J. J., & Wiley, D. C. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.531 · Cited by 2,706
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
Virus entry: molecular mechanisms and biomedical applications
Dimitrov, D. S. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro817 · Cited by 701
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
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Metadata
- Authors
- Carr, C. M., Chaudhry, C., & Kim, P. S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1997-12-23
- Volume
- 94
- Issue
- 26
- Pages
- 14306-14313
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1986152551
- Cited by
- 401
- References
- 4
- FWCI
- 16.69
- Type
- journal article
- Language
- en
- Open access
- green
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- Carr, C. M., Chaudhry, C., & Kim, P. S. (1997). Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.94.26.14306
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