In mice, cyclic di-GMP is an effective mucosal pneumococcal vaccine adjuvant that stimulates the immune response via two distinct mechanisms.

Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

A newfound signaling enzyme that diverged from a protein family ubiquitous in bacteria provides mechanistic insights into how new signaling activity emerges to control distinct cellular function and physiology.

Subpopulations of polysaccharide producer and surface explorer cells play specialized roles in early Pseudomonas aeruginosa biofilm formation.

Building on previous work (Chatterjee et al., 2014), the mechanism of coincidence detection in bacterial second messenger signaling across membranes is revealed at a molecular level, providing insight into the regulation of a conserved transmembrane receptor.

Precise control of the bacterial flagellar motor determines bacterial cell dispersal and bacteria-surface interactions.

c-di-GMP and HipH function as a toxin-antitoxin-like module to regulate persister cell formation in bacterial biofilms.

The diguanylate cyclase activity of SiaD is activated by its binding partner SiaC thourgh a dynamic mechanism of promoting the formation of active SiaD dimers.

A systematical study of pslG mutants at both a single cell and community level reveals the importance of intracellular glycosyl hydrolase PslG on the cell fate and biofilm development of P. aeruginosa, an opportunistic pathogen that can cause persistent infections.