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Cited by 36Biochemical and Structural CharacterizationBacterial Infections and VaccinesBacterial Genetics and Biotechnology

Chromosomal Expression of the Haemophilus influenzae Hap Autotransporter Allows Fine-Tuned Regulation of Adhesive Potential via Inhibition of Intermolecular Autoproteolysis

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Fink, Doran L., St. Geme, Joseph W.·2003·Journal of Bacteriology
DOI 10.1128/jb.185.5.1608-1615.2003PMC PMC148083
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Abstract

The Haemophilus influenzae Hap autotransporter is a nonpilus adhesin that promotes adherence to respiratory epithelial cells and selected extracellular matrix proteins and facilitates bacterial aggregation and microcolony formation. Hap consists of a 45-kDa outer membrane translocator domain called Hap(beta) and a 110-kDa extracellular passenger domain called Hap(S). All adhesive activity resides within Hap(S), which also contains protease activity and directs its own secretion from the bacterial cell surface via intermolecular autoproteolysis. In the present study, we sought to determine the relationship between the magnitude of Hap expression, the efficiency of Hap autoproteolysis, and the level of Hap-mediated adherence and aggregation. We found that a minimum threshold of Hap precursor was required for autoproteolysis and that this threshold approximated expression of Hap from a chromosomal allele, as occurs in H. influenzae clinical isolates. Chromosomal expression of wild-type Hap was sufficient to promote significant adherence to epithelial cells and extracellular matrix proteins, and adherence was enhanced substantially by inhibition of autoproteolysis. In contrast, chromosomal expression of Hap was sufficient to promote bacterial aggregation only when autoproteolysis was inhibited, indicating that the threshold for Hap-mediated aggregation is above the threshold for autoproteolysis. These results highlight the critical role of autoproteolysis and an intermolecular mechanism of cleavage in controlling the diverse adhesive activities of Hap.

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  • Because Hap can be cleaved from the cell surface, the aggregation interface can be depolymerised to allow bacteria to escape from microcolonies or biofilm.

    “As Hap can be cleaved from the cell surface, this allows for a mechanism whereby the aggregation interface can be depolymerised to allow bacteria to escape from microcolonies or biofilm [87].”

    From Bacterial autoaggregation (2018) · cites this paper as [87]

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Authors
Fink, D. L., & St. Geme, J. W.
Affiliations
  • St. Louis Children's Hospital (US)
  • Edward Mallinckrodt Department of Pediatrics and Department of Molecular Microbiology, Washington University School of Medicine, and Division of Infectious Diseases, St. Louis Children's Hospital, St. Louis, Missouri 63110
Venue
Journal of Bacteriology
Publisher
American Society for Microbiology
Published
2003-03
Volume
185
Issue
5
Pages
1608-1615
ISSN
  • 0021-9193 (ISSN-L)
  • 1098-5530
DOI
10.1128/jb.185.5.1608-1615.2003
PMC
PMC148083
OpenAlex
W2123839461
Cited by
36
References
20
Citations by year
2026: 1 · 2021: 1 · 2018: 2 · 2017: 1 · 2015: 2 · 2014: 2 · 2013: 2 · 2012: 3
FWCI
1.38
Type
journal article
Language
en
Open access
Licence
journals.asm.org/non-commercial-tdm-license (tdm)
Locations
  • Journal of Bacteriology (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
Funders
American Heart Association
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Life Sciences › Immunology and Microbiology › Microbiology › Bacterial Infections and Vaccines
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Keywords
Haemophilus influenzae, bacterial adhesion, bacterial aggregation, passenger domain, proteolytic activity, extracellular matrix proteins, airway epithelial cells, microcolony formation
MeSH terms
Bacterial Adhesion, Bacterial Outer Membrane Proteins, Bacterial Proteins, Carrier Proteins, Cells, Cultured, Chromosomes, Bacterial, Epithelial Cells, Haemophilus influenzae, Humans, Proteins, Serine Endopeptidases, Gene Expression Regulation, Bacterial, Threshold Limit Values, Proteinase Inhibitory Proteins, Secretory

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