HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1.
Publication
, Journal Article
Harris, AK; Bartesaghi, A; Milne, JLS; Subramaniam, S
Published in: Journal of Virology
June 2013
We describe cryo-electron microscopic studies of the interaction between the ectodomain of the trimeric HIV-1 envelope glycoprotein (Env) and Z13e1, a broadly neutralizing antibody that targets the membrane-proximal external region (MPER) of the gp41 subunit. We show that Z13e1-bound Env displays an open quaternary conformation similar to the CD4-bound conformation. Our results support the idea that MPER-directed antibodies, such as Z13e1, block viral entry by interacting with Env at a step after CD4 activation.
Duke Scholars
Published In
Journal of Virology
DOI
EISSN
1098-5514
ISSN
0022-538X
Publication Date
June 2013
Volume
87
Issue
12
Start / End Page
7191 / 7196
Related Subject Headings
- env Gene Products, Human Immunodeficiency Virus
- Virology
- Protein Multimerization
- Protein Conformation
- Protein Binding
- Neutralization Tests
- Models, Molecular
- Humans
- HIV Envelope Protein gp41
- Cryoelectron Microscopy
Citation
APA
Chicago
ICMJE
MLA
NLM
Harris, A. K., Bartesaghi, A., Milne, J. L. S., & Subramaniam, S. (2013). HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. Journal of Virology, 87(12), 7191–7196. https://doi.org/10.1128/jvi.03284-12
Harris, Audray K., Alberto Bartesaghi, Jacqueline L. S. Milne, and Sriram Subramaniam. “HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1.” Journal of Virology 87, no. 12 (June 2013): 7191–96. https://doi.org/10.1128/jvi.03284-12.
Harris AK, Bartesaghi A, Milne JLS, Subramaniam S. HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. Journal of Virology. 2013 Jun;87(12):7191–6.
Harris, Audray K., et al. “HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1.” Journal of Virology, vol. 87, no. 12, June 2013, pp. 7191–96. Epmc, doi:10.1128/jvi.03284-12.
Harris AK, Bartesaghi A, Milne JLS, Subramaniam S. HIV-1 envelope glycoprotein trimers display open quaternary conformation when bound to the gp41 membrane-proximal external-region-directed broadly neutralizing antibody Z13e1. Journal of Virology. 2013 Jun;87(12):7191–7196.
Published In
Journal of Virology
DOI
EISSN
1098-5514
ISSN
0022-538X
Publication Date
June 2013
Volume
87
Issue
12
Start / End Page
7191 / 7196
Related Subject Headings
- env Gene Products, Human Immunodeficiency Virus
- Virology
- Protein Multimerization
- Protein Conformation
- Protein Binding
- Neutralization Tests
- Models, Molecular
- Humans
- HIV Envelope Protein gp41
- Cryoelectron Microscopy