Evidence map›Paper›PMID 11029419›Full record

ArticleJournal of bacteriology2000

The Haemophilus influenzae Hia adhesin is an autotransporter protein that remains uncleaved at the C terminus and fully cell associated.

J W St Geme, D Cutter

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.6field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

50 citing papers in PubMed, 109 citations in OpenAlex.

  1. The role of adhesins ofGut microbes · 2026
    Review
  2. Review
  3. Journal of bacteriology · 2026
    Review
  4. Article
  5. Genomic Analysis ofMicroorganisms · 2021
    Article
  6. Non-TypeableInternational journal of molecular sciences · 2020
    Article
  7. Utilizing WholeJournal of bacteriology · 2019
    Article
  8. Molecular Mechanisms ofFrontiers in cellular and infection microbiology · 2018
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Complete fiber structures of complex trimeric autotransporter adhesins conserved in enterobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

J W St GemeEdward Mallinckrodt Department of Pediatrics and Department of Molecular Microbiology, Washington University School of Medicine, St. Louis Children's Hospital, St. Louis, Missouri 63110, USA. srgeme@borcim.wustl.edu
D Cutter
Mallinckrodt (United States) · US

Funding

BIOLOGY OF THE HMW2 AND HMW2 ADHESINS OF H INFLUENZAER01DC002873 · NIDCD · WASHINGTON UNIVERSITY · PI ST. GEME, JOSEPH W. · 1995 to 2014
$4.4M
BIOLOGY OF H INFLUENZAE HIA AND HSF ADHESINSR01AI044167 · NIAID · WASHINGTON UNIVERSITY · PI ST. GEME, JOSEPH W. · 1999 to 2008
$2.5M
NIAID NIH HHS 1RO1 AI-44167NIAID NIH HHS R01 AI044167NIDCD NIH HHS 1RO1 DC-02873NIDCD NIH HHS R01 DC002873
6 · The paper itself

Abstract

Nontypeable Haemophilus influenzae is a gram-negative commensal organism that is commonly associated with localized respiratory tract disease. The pathogenesis of disease begins with colonization of the nasopharynx, a process that likely depends on bacterial adherence to respiratory epithelial cells. Hia is the major adhesin expressed by a subset of nontypeable H. influenzae strains and promotes efficient adherence to a variety of human epithelial cell lines. Based on previous work, Hia is transported to the surface of Escherichia coli transformants and is capable of mediating E. coli adherence without the assistance of other H. influenzae proteins. In the present study, we examined the mechanism of Hia secretion. PhoA fusions, deletional mutagenesis, and N-terminal amino acid sequencing established that the signal for Hia export from the cytoplasm resides in the first 49 amino acids, including a 24-amino-acid stretch with striking similarity to the N terminus of a number of proteins belonging to the autotransporter family. Immunoelectron microscopy demonstrated that the Hia internal region defined by amino acids 221 to 779 is exposed on the bacterial surface. Secondary-structure analysis predicted that the C terminus of Hia forms a beta-barrel with a central hydrophilic channel, and site-specific mutagenesis and fusion protein analysis demonstrated that the C terminus targets Hia to the outer membrane and functions as an outer membrane translocator, analogous to observations with autotransporter proteins. In contrast to typical autotransporter proteins, Hia undergoes no cleavage between the internal and C-terminal domains and remains fully cell associated. Together, these results suggest that Hia is the prototype of an important subfamily of autotransporter proteins.

Indexed as

Adhesins, BacterialAlkaline PhosphataseAnimalsArtificial Gene FusionBacterial AdhesionBacterial Outer Membrane ProteinsCell LineChimeraCyclin-Dependent KinasesEscherichia coliEscherichia coli ProteinsHaemophilus influenzaeImmunohistochemistryMutagenesis, Site-DirectedTransformation, BacterialAdhesins, BacterialAlkaline PhosphataseBacterial Outer Membrane ProteinsCyclin-Dependent KinasesEscherichia coli ProteinsphoA protein, E coli

Identifiers

PMID11029419
PMCPMC94733
OpenAlexW2161088806

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.