L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine.
- Author:
Begum AKUZUM
1
;
Sinae KIM
;
Tam Thanh NGUYEN
;
Jeawoo HONG
;
Siyoung LEE
;
Eunhye KIM
;
Joohee KIM
;
Yeook CHOI
;
Hyunjhung JHUN
;
Youngmin LEE
;
Hyunwoo KIM
;
Dong Hyun SOHN
;
Soohyun KIM
Author Information
- Publication Type:Original Article
- Keywords: Papillomaviridae; L1 capsid proteins; Recombinant proteins; Enzyme-linked immunosorbent assay; Western blot
- MeSH: Adolescent; Blotting, Western; Capsid Proteins; Condylomata Acuminata; Enzyme-Linked Immunosorbent Assay; Escherichia coli; Female; Horseradish Peroxidase; Humans; Methods; Papillomaviridae; Recombinant Proteins*; Uterine Cervical Neoplasms; Vaginal Neoplasms
- From:Immune Network 2018;18(3):e19-
- CountryRepublic of Korea
- Language:English
- 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 purified 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.
