Type II secretion systems (T2SSs) promote secretion of folded proteins playing important
roles in nutrient acquisition, adaptation and virulence of Gram‐negative bacteria. Protein …

Type II secretion system (T 2 SS) is a multiprotein trans‐envelope complex that translocates
fully folded proteins through the outer membrane of G ram‐negative bacteria. Although T 2 …

Type 1 pilus biogenesis was used as a paradigm to investigate ordered macromolecular
assembly at the outer cell membrane. The ability of Gram-negative bacteria to secrete …

In G ram‐negative bacteria, type IV pilus assembly (T4PS) and type II secretion (T2SS)
systems polymerize inner membrane proteins called major pilins or pseudopilins …

In Gram‐negative bacteria, type II secretion systems (T2SS) assemble inner membrane
proteins of the major pseudopilin PulG (GspG) family into periplasmic filaments, which could …

The assembly of surface structures in gram-negative bacteria requires specialized secretion
and chaperone systems localized on both sides of the cytoplasmic membrane. Major …

Extracellular fibers called chaperone-usher pathway pili are critical virulence factors in a
wide range of Gram-negative pathogenic bacteria that facilitate binding and invasion into …

Type IV pili are extracellular polymers of the major pilin subunit. These subunits are held
together in the pilus filament by hydrophobic interactions among their N-terminal α-helices …

The type II secretion system (T2SS) is present in many Gram-negative bacteria and is
responsible for secreting a large number of folded proteins, including major virulence …

Type IV pili (T4P) contain hundreds of major subunits, but minor subunits are also required
for assembly and function. Here we show that Pseudomonas aeruginosa minor pilins prime …