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Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development
Influenza viruses A and B are important human respiratory pathogens causing seasonal, endemic and pandemic infections in several parts of the globe with high morbidity and considerable mortality. The current inactivated and live attenuated vaccines are not effective. Therefore, it is of interest to...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Biomedical Informatics
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6077822/ https://www.ncbi.nlm.nih.gov/pubmed/30108413 http://dx.doi.org/10.6026/97320630014183 |
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author | Sankar, Sathish Ramamurthy, Mageshbabu Suganya, Subramanian Nandagopal, Balaji Sridharan, Gopalan |
author_facet | Sankar, Sathish Ramamurthy, Mageshbabu Suganya, Subramanian Nandagopal, Balaji Sridharan, Gopalan |
author_sort | Sankar, Sathish |
collection | PubMed |
description | Influenza viruses A and B are important human respiratory pathogens causing seasonal, endemic and pandemic infections in several parts of the globe with high morbidity and considerable mortality. The current inactivated and live attenuated vaccines are not effective. Therefore, it is of interest to design universal influenza virus vaccines with high efficacy. The peptide GQSVVSVKLAGNSSL of pandemic influenza, the peptide DKTSVTLAGNSSLCS of seasonal influenza and the peptide DILLKFSPTEITAPT of influenza B were identified as potential linear cell mediated epitopes. The epitopes predicted by BepiPred (B-cell epitope designer) program was subjected to docking experiment-using HexDock and CABS dock programs. The epitopes of pandemic H1N1 influenza A gave similar score of high affinity in docking. The epitope DKTSVTLAGNSSLCS of seasonal influenza A and epitope DILLKFSPTEITAPT of influenza B had high binding energy. It is further observed that the peptides GQSVVSVKLAGNSSL (pandemic influenza), DKTSVTLAGNSSLCS (seasonal influenza) DILLKFSPTEITAPT (influenza B) are found to interact with some known MHC class II alleles. These peptides have high-affinity binding with known MHC class II alleles. Thus, they have the potential to elicit cell immune response. These vaccines have to be further evaluated in animal models and human volunteers. These findings have application in the development of peptide B-cell epitope vaccines against influenza viruses. |
format | Online Article Text |
id | pubmed-6077822 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Biomedical Informatics |
record_format | MEDLINE/PubMed |
spelling | pubmed-60778222018-08-14 Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development Sankar, Sathish Ramamurthy, Mageshbabu Suganya, Subramanian Nandagopal, Balaji Sridharan, Gopalan Bioinformation Hypothesis Influenza viruses A and B are important human respiratory pathogens causing seasonal, endemic and pandemic infections in several parts of the globe with high morbidity and considerable mortality. The current inactivated and live attenuated vaccines are not effective. Therefore, it is of interest to design universal influenza virus vaccines with high efficacy. The peptide GQSVVSVKLAGNSSL of pandemic influenza, the peptide DKTSVTLAGNSSLCS of seasonal influenza and the peptide DILLKFSPTEITAPT of influenza B were identified as potential linear cell mediated epitopes. The epitopes predicted by BepiPred (B-cell epitope designer) program was subjected to docking experiment-using HexDock and CABS dock programs. The epitopes of pandemic H1N1 influenza A gave similar score of high affinity in docking. The epitope DKTSVTLAGNSSLCS of seasonal influenza A and epitope DILLKFSPTEITAPT of influenza B had high binding energy. It is further observed that the peptides GQSVVSVKLAGNSSL (pandemic influenza), DKTSVTLAGNSSLCS (seasonal influenza) DILLKFSPTEITAPT (influenza B) are found to interact with some known MHC class II alleles. These peptides have high-affinity binding with known MHC class II alleles. Thus, they have the potential to elicit cell immune response. These vaccines have to be further evaluated in animal models and human volunteers. These findings have application in the development of peptide B-cell epitope vaccines against influenza viruses. Biomedical Informatics 2018-05-31 /pmc/articles/PMC6077822/ /pubmed/30108413 http://dx.doi.org/10.6026/97320630014183 Text en © 2018 Biomedical Informatics http://creativecommons.org/licenses/by/3.0/ This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License. |
spellingShingle | Hypothesis Sankar, Sathish Ramamurthy, Mageshbabu Suganya, Subramanian Nandagopal, Balaji Sridharan, Gopalan Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title | Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title_full | Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title_fullStr | Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title_full_unstemmed | Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title_short | Design of peptide epitope from the neuraminidase protein of influenza A and influenza B towards short peptide vaccine development |
title_sort | design of peptide epitope from the neuraminidase protein of influenza a and influenza b towards short peptide vaccine development |
topic | Hypothesis |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6077822/ https://www.ncbi.nlm.nih.gov/pubmed/30108413 http://dx.doi.org/10.6026/97320630014183 |
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