Publication: Chimeric hepatitis E virus-like particle as a carrier for oral-delivery
2
Issued Date
2013-01-02
Resource Type
ISSN
18732518
0264410X
0264410X
Other identifier(s)
2-s2.0-84871376730
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Mahidol University
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SCOPUS
Bibliographic Citation
Vaccine. Vol.31, No.2 (2013), 417-424
Suggested Citation
Pitchanee Jariyapong, Li Xing, Nienke E. van Houten, Tian Cheng Li, Wattana Weerachatyanukul, Benjamin Hsieh, Carlos G. Moscoso, Chun Chieh Chen, Masahiro Niikura, Holland H.R. Cheng Chimeric hepatitis E virus-like particle as a carrier for oral-delivery. Vaccine. Vol.31, No.2 (2013), 417-424. doi:10.1016/j.vaccine.2012.10.073 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/31380
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Title
Chimeric hepatitis E virus-like particle as a carrier for oral-delivery
Abstract
Oral delivery with virus-like particles (VLPs) is advantageous because of the inherited entry pathway from their parental viral capsids, which enables VLP to withstand the harsh and enzymatic environment associated with human digestive tract. However, the repeat use of this system is challenged by the self-immunity. In order to overcome this problem, we engineered the recombinant capsid protein of hepatitis E virus by inserting p18 peptide, derived from the V3 loop of HIV-1 gp120, into the antibody-binding site. The chimeric VLP resembled the tertiary and quaternary structures of the wild type VLP and specifically reacted with an HIV-1 antibody against V3 loop. Different from the wild type VLP, the chimeric VLP was vulnerable to trypsin cleavage although it appeared as intact particle, suggesting that the intermolecular forces of attraction between the recombinant capsid proteins are strong enough to maintain the VLP icosahedral arrangement. Importantly, this VLP containing the V3 loop did not react with anti-HEV antibodies, in correspondence to the mutation at its antibody-binding site. Therefore, the insertion of peptides at the surface antigenic site could allow VLPs to escape pre-existing anti-HEV humoral immunity. © 2012 Elsevier Ltd.