3 years ago

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

Structure of the staphylococcal enterotoxin B vaccine candidate S19 showing eliminated superantigen activity
Woo Hyeon Jeong, Dong Hyun Song, Seong Tae Jeong, Gyeung Haeng Hur
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.Mutations introduced into S19, a recombinant staphylococcal enterotoxin B vaccine candidate, contribute to its reduced cytokine induction in vivo by removing hydrogen bonds and allowing interaction with the T-cell receptor beta chain and major histocompatibility complex class II.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1107/S2053230X17014844

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