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. 1996 Oct 15;93(21):11913–11918. doi: 10.1073/pnas.93.21.11913

Haemophilus influenzae pili are composite structures assembled via the HifB chaperone.

J W St Geme 1, J S Pinkner 3rd 1, G P Krasan 1, J Heuser 1, E Bullitt 1, A L Smith 1, S J Hultgren 1
PMCID: PMC38158  PMID: 8876237

Abstract

Haemophilus influenzae is a Gram-negative bacterium that represents a common cause of human disease. Disease due to this organism begins with colonization of the upper respiratory mucosa, a process facilitated by adhesive fibers called pili. In the present study, we investigated the structure and assembly of H. influenzae pili. Examination of pili by electron microscopy using quick-freeze, deep-etch and immunogold techniques revealed the presence of two distinct subassemblies, including a flexible two-stranded helical rod comprised of HifA and a short, thin, distal tip structure containing HifD. Genetic and biochemical studies demonstrated that the biogenesis of H. influenzae pili is dependent on a periplasmic chaperone called HifB, which belongs to the PapD family of immunoglobulin-like chaperones. HifB bound directly to HifA and HifD, forming HifB-HifA and HifB-HifD complexes, which were purified from periplasmic extracts by ion-exchange chromatography. Continued investigation of the biogenesis of H. influenzae pili should provide general insights into organelle development and may suggest novel strategies for disease prevention.

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