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L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine

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,...

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Autores principales: Akuzum, Begum, Kim, Sinae, Nguyen, Tam Thanh, Hong, Jeawoo, Lee, Siyoung, Kim, Eunhye, Kim, Joohee, Choi, Yeook, Jhun, Hyunjhung, Lee, Youngmin, Kim, Hyunwoo, Sohn, Dong Hyun, Kim, Soohyun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Korean Association of Immunologists 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026689/
https://www.ncbi.nlm.nih.gov/pubmed/29984037
http://dx.doi.org/10.4110/in.2018.18.e19
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author Akuzum, Begum
Kim, Sinae
Nguyen, Tam Thanh
Hong, Jeawoo
Lee, Siyoung
Kim, Eunhye
Kim, Joohee
Choi, Yeook
Jhun, Hyunjhung
Lee, Youngmin
Kim, Hyunwoo
Sohn, Dong Hyun
Kim, Soohyun
author_facet Akuzum, Begum
Kim, Sinae
Nguyen, Tam Thanh
Hong, Jeawoo
Lee, Siyoung
Kim, Eunhye
Kim, Joohee
Choi, Yeook
Jhun, Hyunjhung
Lee, Youngmin
Kim, Hyunwoo
Sohn, Dong Hyun
Kim, Soohyun
author_sort Akuzum, Begum
collection PubMed
description 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.
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spelling pubmed-60266892018-07-06 L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine Akuzum, Begum Kim, Sinae Nguyen, Tam Thanh Hong, Jeawoo Lee, Siyoung Kim, Eunhye Kim, Joohee Choi, Yeook Jhun, Hyunjhung Lee, Youngmin Kim, Hyunwoo Sohn, Dong Hyun Kim, Soohyun Immune Netw Original Article 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. The Korean Association of Immunologists 2018-06-04 /pmc/articles/PMC6026689/ /pubmed/29984037 http://dx.doi.org/10.4110/in.2018.18.e19 Text en Copyright © 2018. The Korean Association of Immunologists https://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (https://creativecommons.org/licenses/by-nc/4.0/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Article
Akuzum, Begum
Kim, Sinae
Nguyen, Tam Thanh
Hong, Jeawoo
Lee, Siyoung
Kim, Eunhye
Kim, Joohee
Choi, Yeook
Jhun, Hyunjhung
Lee, Youngmin
Kim, Hyunwoo
Sohn, Dong Hyun
Kim, Soohyun
L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title_full L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title_fullStr L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title_full_unstemmed L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title_short L1 Recombinant Proteins of HPV Tested for Antibody Forming Using Sera of HPV Quadrivalent Vaccine
title_sort l1 recombinant proteins of hpv tested for antibody forming using sera of hpv quadrivalent vaccine
topic Original Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6026689/
https://www.ncbi.nlm.nih.gov/pubmed/29984037
http://dx.doi.org/10.4110/in.2018.18.e19
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