Craig D. Ellermeier

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 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 study identifies two glycosyltransferases involved in synthesizing glycolipids in C. difficile and highlights their role in bacterial physiology.

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.