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Open AccessArticle

T = 4 Icosahedral HIV-1 Capsid As an Immunogenic Vector for HIV-1 V3 Loop Epitope Display

1
State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, China
2
National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Life Sciences, Xiamen University, Xiamen 361102, China
3
Department of Chemistry and Biochemistry and Division of Biological Sciences, University of California-San Diego, San Diego, CA 92093-0378, USA
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2018, 10(12), 667; https://doi.org/10.3390/v10120667
Received: 17 October 2018 / Revised: 21 November 2018 / Accepted: 23 November 2018 / Published: 26 November 2018
(This article belongs to the Section Animal Viruses)
The HIV-1 mature capsid (CA) assumes an amorphous, fullerene conical configuration due to its high flexibility. How native CA self-assembles is still unclear despite having well-defined structures of its pentamer and hexamer building blocks. Here we explored the self-assembly of an engineered capsid protein built through artificial disulfide bonding (CA N21C/A22C) and determined the structure of one fraction of the globular particles. CA N21C/A22C was found to self-assemble into particles in relatively high ionic solutions. These particles contained disulfide-bonding hexamers as determined via non-reducing SDS-PAGE, and exhibited two major components of 57.3 S and 80.5 S in the sedimentation velocity assay. Particles had a globular morphology, approximately 40 nm in diameter, in negative-staining TEM. Through cryo-EM 3-D reconstruction, we determined a novel T = 4 icosahedral structure of CA, comprising 12 pentamers and 30 hexamers at 25 Å resolution. We engineered the HIV-1 V3 loop to the CA particles, and found the resultant particles resembled the morphology of their parental particles in TEM, had a positive reaction with V3-specific neutralizing antibodies, and conferred neutralization immunogenicity in mice. Our results shed light on HIV CA assembly and provide a particulate CA for epitope display. View Full-Text
Keywords: HIV-1 capsid; T = 4 icosahedral; assembly; cryo electron microscopy; epitope display HIV-1 capsid; T = 4 icosahedral; assembly; cryo electron microscopy; epitope display
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Zhang, Z.; He, M.; Bai, S.; Zhang, F.; Jiang, J.; Zheng, Q.; Gao, S.; Yan, X.; Li, S.; Gu, Y.; Xia, N. T = 4 Icosahedral HIV-1 Capsid As an Immunogenic Vector for HIV-1 V3 Loop Epitope Display. Viruses 2018, 10, 667.

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