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Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1
Open accessPublished version of a preprint
Abstract
A central goal of HIV-1 vaccine research is the elicitation of antibodies capable of neutralizing diverse primary isolates of HIV-1. Here we show that focusing the immune response to exposed N-terminal residues of the fusion peptide, a critical component of the viral entry machinery and the epitope of antibodies elicited by HIV-1 infection, through immunization with fusion peptide-coupled carriers and prefusion stabilized envelope trimers, induces cross-clade neutralizing responses. In mice, these immunogens elicited monoclonal antibodies capable of neutralizing up to 31% of a cross-clade panel of 208 HIV-1 strains. Crystal and cryoelectron microscopy structures of these antibodies revealed fusion peptide conformational diversity as a molecular explanation for the cross-clade neutralization. Immunization of guinea pigs and rhesus macaques induced similarly broad fusion peptide-directed neutralizing responses, suggesting translatability. The N terminus of the HIV-1 fusion peptide is thus a promising target of vaccine efforts aimed at eliciting broadly neutralizing antibodies. An alternative HIV vaccine design facilitates generation of HIV-1-antibodies, with promising neutralization breadth in rodents and nonhuman primates.
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Metadata
- Authors
- Xu, K., Acharya, P., Kong, R., Cheng, C., Chuang, G.-Y., Liu, K., Louder, M. K., O’Dell, S., Rawi, R., Sastry, M., Shen, C.-H., Zhang, B., Zhou, T., Asokan, M., Bailer, R. T., Chambers, M., Chen, X., Choi, C. W., Dandey, V. P., Doria-Rose, N. A., Druz, A., Eng, E. T., Farney, S. K., Foulds, K. E., Geng, H., Georgiev, I. S., Gorman, J., Hill, K. R., Jafari, A. J., Kwon, Y. D., Lai, Y.-T., Lemmin, T., McKee, K., Ohr, T. Y., Ou, L., Peng, D., Rowshan, A. P., Sheng, Z., Todd, J.-P., Tsybovsky, Y., Viox, E. G., Wang, Y., Wei, H., Yang, Y., Zhou, A. F., Chen, R., Yang, L., Scorpio, D. G., McDermott, A. B., Shapiro, L., Carragher, B., Potter, C. S., Mascola, J. R., & Kwong, P. D.
- Venue
- Nature Medicine
- Published
- 2018-06
- Volume
- 24
- Issue
- 6
- Pages
- 857-867
- ISSN
- 1078-8956 (ISSN-L)
- 1546-170X
- OpenAlex
- W2799119185
- Cited by
- 283
- References
- 82
- FWCI
- 19.27
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.springernature.com/gp/researchers/text-and-data-mining (tdm)
- www.springernature.com/gp/researchers/text-and-data-mining (vor)
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- Xu, K., Acharya, P., Kong, R., Cheng, C., Chuang, G.-Y., Liu, K., Louder, M. K., O’Dell, S., Rawi, R., Sastry, M., Shen, C.-H., Zhang, B., Zhou, T., Asokan, M., Bailer, R. T., Chambers, M., Chen, X., Choi, C. W., Dandey, V. P., . . . Kwong, P. D. (2018). Epitope-based vaccine design yields fusion peptide-directed antibodies that neutralize diverse strains of HIV-1. Nature Medicine. https://doi.org/10.1038/s41591-018-0042-6
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