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PMID: 8876237 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

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

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 93 ·No. 21 ·1996-10-15 ·Pages 11913-8

St Geme JW, Pinkner JS, Krasan GP, Heuser J, Bullitt E, Smith AL, Hultgren SJ

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.

MeSH Terms
Bacterial Outer Membrane Proteins/metabolism,ultrastructure Bacterial Proteins/metabolism,physiology,ultrastructure Cell Fractionation Fimbriae Proteins Fimbriae, Bacterial/physiology,ultrastructure Freeze Etching Gene Deletion Genes, Bacterial Haemophilus influenzae/genetics,physiology,ultrastructure Humans Influenza, Human/microbiology,prevention & control Microscopy, Electron Microscopy, Immunoelectron Molecular Chaperones/physiology,ultrastructure Mutagenesis Protein Binding
Chemicals
Bacterial Outer Membrane Proteins Bacterial Proteins HifA protein, Haemophilus influenzae HifB protein, Haemophilus influenzae HifD protein, Haemophilus influenzae Molecular Chaperones Fimbriae Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
St Geme J W
Edward Mallinckrodt Department of Pediatrics, Washington University School of Medicine, St. Louis, MO 63110, USA. [email protected]
Pinkner J S
Krasan G P
Heuser J
Bullitt E
Smith A L
Hultgren S J
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.93.21.11913
Email
[email protected]
Published
1996-10-15
Pages
11913-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC38158
Subset
IM
Grants
NIAID NIH HHS · AI29549 · United States
External Links
PubMed source DOI: 10.1073/pnas.93.21.11913 PMC Full Text View journal details
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