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Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity
Author(s) -
Jeong Woo Hyeon,
Song Dong Hyun,
Hur Gyeung Haeng,
Jeong Seong Tae
Publication year - 2017
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x17014844
Subject(s) - superantigen , enterotoxin , microbiology and biotechnology , staphylococcus aureus , virology , biology , genetics , escherichia coli , gene , bacteria
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.