The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Evidence That the Transition of HIV-1 Gp41 into a Six-Helix Bundle, Not the Bundle Configuration, Induces Membrane Fusion
Open accessAbstract
Many viral fusion proteins exhibit a six-helix bundle as a core structure. HIV Env–induced fusion was studied to resolve whether membrane merger was due to the transition into the bundle configuration or occurred after bundle formation. Suboptimal temperature was used to arrest fusion at an intermediate stage. When bundle formation was prevented by adding inhibitory peptides at this stage, membranes did not merge upon raising temperature. Inversely, when membrane merger was prevented by incorporating lysophosphatidylcholine (LPC) into cell membranes at the intermediate, the bundle did not form upon optimizing temperature. In the absence of LPC, the six-helix bundle did not form when the temperature of the intermediate was raised for times too short to promote fusion. Kinetic measures showed that after the temperature pulse, cells had not advanced further toward fusion. The latter results indicate that bundle formation is the rate-limiting step between the arrested intermediate and fusion. Electrical measures showed that the HIV Env–induced pore is initially large and grows rapidly. It is proposed that bundle formation and fusion are each contingent on the other and that movement of Env during its transition into the six-helix bundle directly induces the lipid rearrangements of membrane fusion. Because peptide inhibition showed that, at the intermediate stage, the heptad repeats of gp41 have become stably exposed, creation of the intermediate could be of importance in drug and/or vaccine development.
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Cites
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
Sutton, R. B., Fasshauer, D., Jahn, R., & Brunger, A. T. (1998) · Nature · doi:10.1038/26412 · Cited by 2,417 · cited 2×
“…may even extend to eukaryotic cells: a complex of soluble N -ethylmaleimide–sensitive factor (NSF) attachment protein receptors (SNAREs), thought to be responsible for intracellular fusion, has been crystallographically shown to form bundle structures (Poirier et al., 1998; Sutton et al., 1998).”
BackgroundChemokine receptors as HIV-1 coreceptors: roles in viral entry, tropism, and disease
Berger, E. A., Murphy, P. M., & Farber, J. M. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.657 · Cited by 2,180
Cited by
Bosch, B. J., van der Zee, R., de Haan, C. A. M., & Rottier, P. J. M. (2003) · Journal of Virology · doi:10.1128/jvi.77.16.8801-8811.2003 · Cited by 1,489
Structure of the dengue virus envelope protein after membrane fusion
Modis, Y., Ogata, S., Clements, D., & Harrison, S. C. (2004) · Nature · doi:10.1038/nature02165 · Cited by 1,203
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
The structural biology of type I viral membrane fusion
Colman, P. M., & Lawrence, M. C. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1076 · Cited by 454
Sanders, R. W., Vesanen, M., Schuelke, N., Master, A., Schiffner, L., Kalyanaraman, R., Paluch, M., Berkhout, B., Maddon, P. J., Olson, W. C., et al. (2002) · Journal of Virology · doi:10.1128/jvi.76.17.8875-8889.2002 · Cited by 440
Metadata
- Authors
- Melikyan, G. B., Markosyan, R. M., Hemmati, H., Delmedico, M. K., Lambert, D. M., & Cohen, F. S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2000-10-16
- Volume
- 151
- Issue
- 2
- Pages
- 413-424
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2168357995
- Cited by
- 576
- References
- 2
- FWCI
- 9.79
- Type
- journal article
- Language
- en
- Open access
- green
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