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Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity
Four mutations (N23A, Y90A, R110A and F177A) were introduced into S19, a vaccine candidate for staphylococcal enterotoxin B (SEB), resulting in a lower binding affinity towards the T-cell receptor beta chain (TCB) and reducing its superantigen activity. The structure of S19 was solved and was superp...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683028/ https://www.ncbi.nlm.nih.gov/pubmed/29095152 http://dx.doi.org/10.1107/S2053230X17014844 |
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author | Jeong, Woo Hyeon Song, Dong Hyun Hur, Gyeung Haeng Jeong, Seong Tae |
author_facet | Jeong, Woo Hyeon Song, Dong Hyun Hur, Gyeung Haeng Jeong, Seong Tae |
author_sort | Jeong, Woo Hyeon |
collection | PubMed |
description | Four mutations (N23A, Y90A, R110A and F177A) were introduced into S19, a vaccine candidate for staphylococcal enterotoxin B (SEB), resulting in a lower binding affinity towards the T-cell receptor beta chain (TCB) and reducing its superantigen activity. The structure of S19 was solved and was superposed on the native or complex structure of SEB. In the superposition model, mutations that were introduced seemed to reduce the number of hydrogen bonds at the SEB–TCB interface. S19 also displayed an unexpected structural change around the flexible-loop region owing to the Y90A mutation. This local structural change provided evidence that the mutated form of S19 could have a lower affinity for major histocompatibility complex (MHC) class II than wild-type SEB. |
format | Online Article Text |
id | pubmed-5683028 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-56830282017-11-17 Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity Jeong, Woo Hyeon Song, Dong Hyun Hur, Gyeung Haeng Jeong, Seong Tae Acta Crystallogr F Struct Biol Commun Research Communications Four mutations (N23A, Y90A, R110A and F177A) were introduced into S19, a vaccine candidate for staphylococcal enterotoxin B (SEB), resulting in a lower binding affinity towards the T-cell receptor beta chain (TCB) and reducing its superantigen activity. The structure of S19 was solved and was superposed on the native or complex structure of SEB. In the superposition model, mutations that were introduced seemed to reduce the number of hydrogen bonds at the SEB–TCB interface. S19 also displayed an unexpected structural change around the flexible-loop region owing to the Y90A mutation. This local structural change provided evidence that the mutated form of S19 could have a lower affinity for major histocompatibility complex (MHC) class II than wild-type SEB. International Union of Crystallography 2017-10-20 /pmc/articles/PMC5683028/ /pubmed/29095152 http://dx.doi.org/10.1107/S2053230X17014844 Text en © Jeong et al. 2017 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Communications Jeong, Woo Hyeon Song, Dong Hyun Hur, Gyeung Haeng Jeong, Seong Tae Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title | Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title_full | Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title_fullStr | Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title_full_unstemmed | Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title_short | Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity |
title_sort | structure of the staphylococcal enterotoxin b vaccine candidate s19 showing eliminated superantigen activity |
topic | Research Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5683028/ https://www.ncbi.nlm.nih.gov/pubmed/29095152 http://dx.doi.org/10.1107/S2053230X17014844 |
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