Kevin E. Bruce

This paper identifies the pneumococcal S protein as essential for resisting host antimicrobials by coordinating cell wall modification and repair through interactions with PBP1a and PgdA.

This study identifies the enzymatic function of PcsB, a peptidoglycan hydrolase in Streptococcus pneumoniae, showing it cleaves Lys-containing, amidated peptidoglycan and is regulated by structural changes.

This study shows that the CRY2/CIB1 system can be used to precisely control protein localization in E. coli, enabling manipulation of cellular functions like cytokinesis.

This study identifies three types of single-molecule motions of PG synthesis proteins in Streptococcus pneumoniae, revealing zonal, circumferential movement of core elongasome proteins and distinct behaviors of aPBP1a and MpgA.