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-Structure paper
Title | Bacterially expressed human papillomavirus type 6 and 11 bivalent vaccine: Characterization, antigenicity and immunogenicity. |
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Journal, issue, pages | Vaccine, Vol. 35, Issue 24, Page 3222-3231, Year 2017 |
Publish date | May 31, 2017 |
Authors | Huirong Pan / Zhihai Li / Jin Wang / Shuo Song / Daning Wang / Minxi Wei / Ying Gu / Jun Zhang / Shaowei Li / Ningshao Xia / |
PubMed Abstract | Human papillomavirus (HPV)-6 and HPV11 are the major etiological causes of condylomata acuminate. HPV neutralization by vaccine-elicited neutralizing antibodies can block viral infection and prevent ...Human papillomavirus (HPV)-6 and HPV11 are the major etiological causes of condylomata acuminate. HPV neutralization by vaccine-elicited neutralizing antibodies can block viral infection and prevent subsequent disease. Currently, two commercially available HPV vaccines cover these two genotypes, expressed by Saccharomyces cerevisiae. Here we describe another HPV6/11 bivalent vaccine candidate derived from Escherichia coli. The soluble expression of N-terminally truncated L1 proteins was optimized to generate HPV6- and HPV11 L1-only virus-like particles (VLPs) as a scalable process. In a pilot scale, we used various biochemical, biophysical and immunochemical approaches to comprehensively characterize the scale and lot consistency of the vaccine candidate at 30L and 100L. Cryo-EM structure analysis showed that these VLPs form a T=7 icosahedral lattice, imitating the L1 capsid of the authentic HPV virion. This HPV6/11 bivalent vaccine confers a neutralization titer and antibody production profile in monkey that is comparable with the quadrivalent vaccine, Gardasil. This study demonstrates the robustness and scalability of a potential HPV6/11 bivalent vaccine using a prokaryotic system for vaccine production. |
External links | Vaccine / PubMed:28483196 |
Methods | EM (single particle) |
Resolution | 20.0 - 30.0 Å |
Structure data | EMDB-6797: EMDB-6798: |