David S. Weiss

This paper identifies DD-CPases as the source of tetrapeptides for LDTs in C. difficile and shows that LDTs are essential due to high DD-CPase activity, not for divisome/elongasome function.

This paper identifies CenIR as an essential BlaIR-family regulatory system in C. difficile that lacks a β-lactam-binding domain and is required for viability, with its regulon containing genes involved in peptidoglycan hydrolase and cell envelope maintenance.

This study identifies MltA as a lytic transglycosylase involved in cleaving septal peptidoglycan during E. coli cell division.

This study identifies essential genes in C. difficile using CRISPRi and Tn-seq, confirming most previously reported genes and identifying new ones, with comparisons to B. subtilis.

This paper shows FtsZ treadmilling acts as a template and conveyor to organize cell wall synthesis during bacterial division, with roles changing over time.

This study identifies a new family of LDTs in C. difficile that catalyze 3-3 peptidoglycan crosslinking, essential for viability and distinct from previously known YkuD domain LDTs.