Immune Netw.
2018 Jun;18(3):e19. 10.4110/in.2018.18.e19.
L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
- Affiliations
-
- 1Laboratory of Cytokine Immunology, Department of Biomedical Science and Technology, Konkuk University, Seoul 05029, Korea. soohyun@konkuk.ac.kr
- 2College of Veterinary Medicine, Konkuk University, Seoul 05029, Korea.
- 3YbdYbiotech Research Center, Seoul 08589, Korea.
- 4Research Group of Nutraceuticals for Metabolic Syndrome, Korea Food Research Institute, Wanju 55365, Korea.
- 5Department of Medicine, Pusan Paik Hospital, Inje University College of Medicine, Busan 47392, Korea.
- 6Division of Nephrology, Department of Internal Medicine, Jeju National University School of Medicine, Jeju 63243, Korea.
- 7Department of Microbiology and Immunology, Pusan National University School of Medicine, Yangsan 50612, Korea.
- KMID: 2414555
- DOI: http://doi.org/10.4110/in.2018.18.e19
Abstract
- Virus-like particles (VLPs) derived from human papillomavirus (HPV) L1 capsid proteins were used for HPV quadrivalent recombinant vaccine. The HPV quadrivalent vaccine is administrated in a 3-dose regimen of initial injection followed by subsequent doses at 2 and 6 months to prevent cervical cancer, vulvar, and vaginal cancers. The type 6, 11, 16, or 18 of HPV infection is associated with precancerous lesions and genital warts in adolescents and young women. The HPV vaccine is composed of viral L1 capsid proteins are produced in eukaryotic expression systems and puriï¬ed in the form of VLPs. Four different the L1 protein of 3 different subtypes of HPV: HPV11, HPV16, and HPV18 were expressed in Escherichia coli divided into 2 fragments as N- and C-terminal of each protein in order to examine the efficacy of HPV vaccine. Vaccinated sera failed to recognize N-terminal L1 HPV type 16 and type 18 by western blot while they detected N-terminal L1 protein of HPV type 11. Moreover, the recombinant C-terminal L1 proteins of type 16 was non-specifically recognized by the secondary antibody conjugated with horseradish peroxidase. This expression and purification system may provide simple method to obtain robust recombinant L1 protein of HPV subtypes to improve biochemical analysis of antigens with immunized sera.
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