Evidence map›Paper›PMID 21841773›Full record

ArticleThe EMBO journal2011

Crystal structure of the Haemophilus influenzae Hap adhesin reveals an intercellular oligomerization mechanism for bacterial aggregation.

Guoyu Meng, Nicole Spahich, Roma Kenjale, Gabriel Waksman, Joseph W St Geme

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

40 citing papers in PubMed, 72 citations in OpenAlex.

  1. ThemBio · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Structural and functional significance of the amino acid differences ValInternational journal of biological macromolecules · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Frontiers in microbiology · 2020
    Article
  14. Article
  15. Bacterial autoaggregation.AIMS microbiology · 2018
    Review
  16. Article
  17. Inactivation of the Thymidylate SynthaseFrontiers in cellular and infection microbiology · 2017
    Article
  18. Review
  19. Review
  20. Article
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

5 authors at 3 institutions in 3 countries.

Guoyu MengState Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, Rui-Jin Hospital affiliated to Shanghai JiaoTong University School of Medicine, PR China. guoyumeng@shsmu.edu.cn
Nicole Spahich
Roma Kenjale
Gabriel Waksman
Joseph W St Geme
Duke University Hospital · USInstitute of Structural and Molecular Biology · GBShanghai Jiao Tong University · CN

Funding

Haemophilus Hap-mediated Microcolony FormationR01AI049322 · NIAID · WASHINGTON UNIVERSITY · PI ST. GEME, JOSEPH W. · 2003 to 2007
$1.1M
Medical Research Council G0800002NIAID NIH HHS R01 AI049322NIAID NIH HHS R01 AI49322
6 · The paper itself

Abstract

Bacterial biofilms are complex microbial communities that are common in nature and are being recognized increasingly as an important determinant of bacterial virulence. However, the structural determinants of bacterial aggregation and eventual biofilm formation have been poorly defined. In Gram-negative bacteria, a major subgroup of extracellular proteins called self-associating autotransporters (SAATs) can mediate cell-cell adhesion and facilitate biofilm formation. In this study, we used the Haemophilus influenzae Hap autotransporter as a prototype SAAT to understand how bacteria associate with each other. The crystal structure of the H. influenzae Hap(S) passenger domain (harbouring the SAAT domain) was determined to 2.2 Å by X-ray crystallography, revealing an unprecedented intercellular oligomerization mechanism for cell-cell interaction. The C-terminal SAAT domain folds into a triangular-prism-like structure that can mediate Hap-Hap dimerization and higher degrees of multimerization through its F1-F2 edge and F2 face. The intercellular multimerization can give rise to massive buried surfaces that are required for overcoming the repulsive force between cells, leading to bacterial cell-cell interaction and formation of complex microcolonies.

Indexed as

Protein MultimerizationBacterial AdhesionBacterial Outer Membrane ProteinsCrystallography, X-RayHaemophilus influenzaeModels, BiologicalModels, MolecularProtein BindingProtein Structure, QuaternarySerine EndopeptidasesBacterial Outer Membrane ProteinsHap protein, Hemophilus influenzaeSerine Endopeptidases

Identifiers

PMID21841773
PMCPMC3173798
OpenAlexW1518421544

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.