Abstract
Type IV pili are long polymers located on the surface of a wide variety of bacterial cells, including the pathogen Neisseria meningitidis. They are responsible for a diverse range of functions, including adhesion, motility and natural transformation. In this issue of The EMBO Journal, Imhaus and Duménil show that two minor pilins, PilX and PilV, exert some of their effects by changing mean surface pilus number and that this modulates different pilus-dependent functions.
Highlights
Type IV pili are long polymers located on the surface of a wide variety of bacterial cells, including the pathogen Neisseria meningitidis
Type IV pili (TFP) are the most widespread class of pili or fimbriae found in bacteria; they have a particular importance in proteobacteria which cause human disease, such as Neisseria meningitidis, the causative agent of meningococcal meningitis, Pseudomonas aeruginosa and enteropathogenic Escherichia coli (Pelicic, 2008)
Type IV pili are predominantly composed of a major pilin protein which adopts a conserved fold, based on a single a-helix packed against a 4-stranded b-sheet
Summary
Type IV pili are long polymers located on the surface of a wide variety of bacterial cells, including the pathogen Neisseria meningitidis. We know little at present to answer these questions, but some pertinent observations from the recent paper from Imhaus and Dumenil (2014) suggests a role for two minor pilins, PilX and PilV, in the process.
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