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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,...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Korean Association of Immunologists
2018
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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. |
format | Online Article Text |
id | pubmed-6026689 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | The Korean Association of Immunologists |
record_format | MEDLINE/PubMed |
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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