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Cited by 76Biochemical and Structural CharacterizationBacterial biofilms and quorum sensingEnzyme Structure and Function

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

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Meng, Guoyu, Spahich, Nicole, Kenjale, Roma, Waksman, Gabriel, St Geme, Joseph W·2011·The EMBO Journal
DOI 10.1038/emboj.2011.279PMC PMC3173798
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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.

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Crossref · 10.1038/emboj.2011.279

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  • Mutating residues in the Asn/Asp ladder of Hap to alanine does not significantly reduce the self-aggregating properties of Hap.

    “It should be noted that mutating residues in the Asn/Asp ladder to alanine does not significantly reduce the self-aggregating properties of Hap.”

    From Bacterial autoaggregation (2018) · cites this paper as [85]

  • Hap aggregation is mediated by van der Waals forces derived from self-complementary interacting surfaces, making multimer formation a low-affinity, entropy-driven interaction.

    “Rather than through direct hydrogen bonding, Meng et al. suggest that the aggregation is mediated by van der Waals forces derived from self-complementary interacting surfaces [85]. Thus, multimer formation should be a low affinity interaction and entropy-driven.”

    From Bacterial autoaggregation (2018) · cites this paper as [85]

  • Soluble Hap monomers in dilute solution do not aggregate.

    “Soluble Hap monomers in dilute solution do not aggregate.”

    From Bacterial autoaggregation (2018) · cites this paper as [85]

  • The extracellular region of the Haemophilus influenzae autotransporter adhesin Hap resembles a "Dane axe", with a protruding protease domain at the N-terminus and a β-helical stalk at the C-terminus.

    “The extracellular region of the Haemophilus influenzae autotransporter adhesin Hap resembles a “Dane axe”, with a protruding protease domain at the N-terminus (the “axe blade”) and a β-helical stalk (the “handle”) at the C-terminus (Figure 2A) [85].”

    From Bacterial autoaggregation (2018) · cites this paper as [85]

  • Dynamic light scattering data show strongly temperature-dependent polymerisation of Hap.

    “This model is supported by dynamic light scattering data, showing strongly temperature-dependent polymerisation [85].”

    From Bacterial autoaggregation (2018) · cites this paper as [85]

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Authors
Meng, G., Spahich, N., Kenjale, R., Waksman, G., & St Geme, J. W.
Affiliations
  • Shanghai Jiao Tong University (CN)
  • Duke University (US)
  • Institute of Structural and Molecular Biology (GB)
Corresponding author
Meng, Guoyu
ORCID
Venue
The EMBO Journal
Publisher
Springer Science and Business Media LLC
Published
2011-08-12
Volume
30
Issue
18
Pages
3864-3874
ISSN
  • 0261-4189 (ISSN-L)
  • 1460-2075
DOI
10.1038/emboj.2011.279
PMC
PMC3173798
OpenAlex
W1518421544
Cited by
76
References
42
Citations by year
2026: 4 · 2025: 1 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 6 · 2020: 2 · 2019: 4 · 2018: 2 · 2017: 2 · 2016: 4 · 2015: 6 · 2014: 12 · 2013: 13 · 2012: 11
FWCI
4.94
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • BIROn (Birkbeck, University of London) (submittedVersion)
  • UCL Discovery (University College London) (submittedVersion)
Funders
  • National Natural Science Foundation of China
  • National Institute of Allergy and Infectious Diseases (R01-AI49322, R01AI049322)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bacterial biofilms and quorum sensing
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
Haemophilus influenzae, bacterial aggregation, cell-cell adhesion, protein oligomerization, biofilm formation, microcolonies, Gram-negative bacteria
MeSH terms
Bacterial Adhesion, Bacterial Outer Membrane Proteins, Haemophilus influenzae, Models, Biological, Models, Molecular, Protein Binding, Serine Endopeptidases, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Multimerization

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