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TitleN-terminal truncations on L1 proteins of human papillomaviruses promote their soluble expression in Escherichia coli and self-assembly in vitro.
Journal, issue, pagesEmerg Microbes Infect, Vol. 7, Issue 1, Page 160, Year 2018
Publish dateSep 26, 2018
AuthorsMinxi Wei / Daning Wang / Zhihai Li / Shuo Song / Xianglin Kong / Xiaobing Mo / Yurou Yang / Maozhou He / Zhongyi Li / Bo Huang / Zhijie Lin / Huirong Pan / Qingbing Zheng / Hai Yu / Ying Gu / Jun Zhang / Shaowei Li / Ningshao Xia /
PubMed AbstractHuman papillomavirus (HPV) is the causative agent in genital warts and nearly all cervical, anogenital, and oropharyngeal cancers. Nine HPV types (6, 11, 16, 18, 31, 33, 45, 52, and 58) are ...Human papillomavirus (HPV) is the causative agent in genital warts and nearly all cervical, anogenital, and oropharyngeal cancers. Nine HPV types (6, 11, 16, 18, 31, 33, 45, 52, and 58) are associated with about 90% of cervical cancers and 90% of genital warts. HPV neutralization by vaccine-elicited neutralizing antibodies can block viral infection and prevent HPV-associated diseases. However, there is only one commercially available HPV vaccine, Gardasil 9, produced from Saccharomyces cerevisiae that covers all nine types, raising the need for microbial production of broad-spectrum HPV vaccines. Here, we investigated whether N-terminal truncations of the major HPV capsid proteins L1, improve their soluble expression in Escherichia coli. We found that N-terminal truncations promoted the soluble expression of HPV 33 (truncated by 10 amino acids [aa]), 52 (15 aa), and 58 (10 aa). The resultant HPV L1 proteins were purified in pentamer form and extensively characterized with biochemical, biophysical, and immunochemical methods. The pentamers self-assembled into virus-like particles (VLPs) in vitro, and 3D cryo-EM reconstructions revealed that all formed T = 7 icosahedral particles having 50-60-nm diameters. Moreover, we formulated a nine-valent HPV vaccine candidate with aluminum adjuvant and L1 VLPs from four genotypes used in this study and five from previous work. Immunogenicity assays in mice and non-human primates indicated that this HPV nine-valent vaccine candidate elicits neutralizing antibody titers comparable to those induced by Gardasil 9. Our study provides a method for producing a nine-valent HPV vaccine in E. coli and may inform strategies for the soluble expression of other vaccine candidates.
External linksEmerg Microbes Infect / PubMed:30254257 / PubMed Central
MethodsEM (single particle)
Resolution7.0 - 12.5 Å
Structure data

EMDB-6909:
CryoEM structure of HPV33 L1-only VLP
Method: EM (single particle) / Resolution: 10.0 Å

EMDB-6910:
CryoEM structure of HPV58 L1-only VLP
Method: EM (single particle) / Resolution: 12.5 Å

EMDB-6918:
CryoEM structure of HPV52 L1-only VLP
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-6919:
CryoEM structure of HPV45 L1-only VLP
Method: EM (single particle) / Resolution: 9.0 Å

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