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Article

Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity.

Acta crystallographica. Section F, Structural biology communications - 1 Nov 2017

Jeong Woo Hyeon, Song Dong Hyun, Hur Gyeung Haeng, Jeong Seong Tae

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Receptors, Antigen, T-Cell, alpha-beta

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Identifiers

PMID: 29095152
DOI: 10.1107/S2053230X17014844
PMCID: PMC5683028

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