The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein

David R. Hendrixson, Joseph W. St. Geme

Research output: Contribution to journalArticle

89 Citations (Scopus)

Abstract

Haemophilus influenzae initiates infection by colonizing the upper respiratory mucosa. The process of colonization involves adherence to epithelium and evasion of host immunity. In this study, we examined the H. influenzae Hap adhesin, which has serine protease activity and undergoes autoproteolytic cleavage and extracellular release in broth. We found that the uncleaved cell-associated form of Hap mediates adherence to cultured epithelial cells and promotes bacterial aggregation and microcolony formation. Adherence and aggregation are augmented by secretory leukocyte protease inhibitor, a natural component of respiratory secretions that inhibits Hap autoproteolysis. These observations suggest a novel paradigm in hostpathogen relations, in which a soluble host protein whose primary function is to protect host epithelium potentiates properties that facilitate bacterial colonization.

Original languageEnglish (US)
Pages (from-to)841-850
Number of pages10
JournalMolecular Cell
Volume2
Issue number6
StatePublished - Dec 1998

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Haemophilus influenzae
Serine Proteases
Epithelium
Secretory Leukocyte Peptidase Inhibitor
Respiratory Mucosa
Cultured Cells
Immunity
Proteins
Epithelial Cells
Infection

ASJC Scopus subject areas

  • Molecular Biology

Cite this

The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein. / Hendrixson, David R.; St. Geme, Joseph W.

In: Molecular Cell, Vol. 2, No. 6, 12.1998, p. 841-850.

Research output: Contribution to journalArticle

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