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Cited by 80Bacterial Infections and VaccinesBiochemical and Structural CharacterizationMicrobial infections and disease research

The Haemophilus influenzae Hap autotransporter mediates microcolony formation and adherence to epithelial cells and extracellular matrix via binding regions in the C-terminal end of the passenger domain

Fink, Doran L., Buscher, Amy Z., Green, Bruce, Fernsten, Phillip, St. Geme, Joseph W.·2003·Cellular Microbiology
DOI 10.1046/j.1462-5822.2003.00266.x
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Abstract

The pathogenesis of non-typable Haemophilus influenzae disease begins with colonization of the nasopharynx and is facilitated by bacterial adherence to respiratory mucosa. The H. influenzae Hap autotransporter is a non-pilus adhesin that promotes adherence to epithelial cells and selected extracellular matrix proteins and mediates bacterial aggregation and microcolony formation. In addition, Hap has serine protease activity. Hap contains a 110 kDa internal passenger domain called HapS and a 45 kDa C-terminal translocator domain called Hapbeta. In the present study, we sought to define the structural basis for Hap adhesive activities. Based on experiments using a panel of monoclonal antibodies against HapS, a deletion derivative lacking most of HapS and a purified fragment of HapS, we established that adherence to epithelial cells is mediated by sequences within the C-terminal 311 residues of HapS. In additional experiments, we discovered that bacterial aggregation is also mediated by sequences within the C-terminal 311 residues of HapS and occurs via HapS-HapS interaction between molecules on neighbouring organisms. Finally, we found that adherence to fibronectin, laminin and collagen IV is mediated in part by sequences within the C-terminal 311 residues of HapS and in full by sequences within the C-terminal 511 residues of HapS. Taken together, these results demonstrate that all Hap adhesive activities reside in the C-terminal portion of HapS. Coupled with earlier observations, the current results establish that HapS adhesive activities and HapS protease activity are contained in separate modules of the protein.

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  • The C-terminal region of Hap harbours the autoaggregative function.

    “The C-terminal region of Hap harbours the autoaggregative function [86].”

    From Bacterial autoaggregation (2018) · cites this paper as [86]

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Authors
Fink, D. L., Buscher, A. Z., Green, B., Fernsten, P., & St. Geme, J. W.
Affiliations
St. Louis Children's Hospital (US)
Venue
Cellular Microbiology
Publisher
Hindawi Limited
Published
2003-03
Volume
5
Issue
3
Pages
175-186
ISSN
  • 1462-5814 (ISSN-L)
  • 1462-5822
DOI
10.1046/j.1462-5822.2003.00266.x
OpenAlex
W2032175820
Cited by
80
References
32
Citations by year
2025: 2 · 2024: 2 · 2022: 1 · 2021: 2 · 2020: 1 · 2019: 3 · 2018: 3 · 2017: 3 · 2016: 4 · 2015: 7 · 2014: 3 · 2013: 4 · 2012: 7
FWCI
3.87
Type
journal article
Language
en
Open access
closed
Licence
doi.wiley.com/10.1002/tdm_license_1.1 (tdm, 4567 d)
Locations
  • Cellular Microbiology (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • American Heart Association
  • National Institutes of Health (7r21ai044322-03)
  • National Institute of Allergy and Infectious Diseases (AI 44322)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Immunology and Microbiology › Microbiology › Microbial infections and disease research
Keywords
Haemophilus influenzae, bacterial adhesion, epithelial cell adherence, extracellular matrix binding, fibronectin, laminin, type IV collagen, microcolony formation, bacterial aggregation, serine protease activity, monoclonal antibodies, nasopharyngeal carriage
MeSH terms
Animals, Antibodies, Monoclonal, Bacterial Adhesion, Bacterial Outer Membrane Proteins, Binding Sites, Carrier Proteins, Cell Line, Epithelial Cells, Extracellular Matrix, Haemophilus influenzae, Models, Molecular, Serine Endopeptidases, Gene Expression Regulation, Bacterial, Protein Structure, Tertiary, Virulence Factors

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