Chimeric hepatitis E virus-like particle as a carrier for oral-delivery
| Autor: | Wattana Weerachatyanukul, Benjamin Hsieh, Carlos G. Moscoso, Masahiro Niikura, Nienke E. van Houten, Holland Cheng, Chun Chieh Chen, Pitchanee Jariyapong, Li Xing, Tian-Cheng Li |
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| Rok vydání: | 2012 |
| Předmět: |
viruses
Recombinant Fusion Proteins Molecular Sequence Data Administration Oral V3 loop Biology HIV Envelope Protein gp120 medicine.disease_cause complex mixtures Article law.invention Virus-like particle Hepatitis E virus law medicine Amino Acid Sequence Hepatitis Antibodies Peptide sequence Antigens Viral Vaccines Binding Sites General Veterinary General Immunology and Microbiology Public Health Environmental and Occupational Health Wild type virus diseases Virology Infectious Diseases Capsid Humoral immunity Recombinant DNA Molecular Medicine Capsid Proteins |
| Zdroj: | Vaccine |
| ISSN: | 1873-2518 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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