Haemophilus influenzae protein E binds to the extracellular matrix by concurrently interacting with laminin and vitronectin |
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Authors: | Hallström Teresia Singh Birendra Resman Fredrik Blom Anna M Mörgelin Matthias Riesbeck Kristian |
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Affiliation: | Medical Microbiology, Department of Laboratory Medicine Malm?, Lund University, Sk?ne University Hospital, Malm?, Sweden. |
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Abstract: | Nontypeable Haemophilus influenzae (NTHi) causes otitis media and is commonly found in patients with chronic obstructive pulmonary disease (COPD). Adhesins are important for bacterial attachment and colonization. Protein E (PE) is a recently characterized ubiquitous 16 kDa adhesin with vitronectin-binding capacity that results in increased survival in serum. In addition to PE, NTHi utilizes Haemophilus adhesion protein (Hap) that binds to the basement-membrane glycoprotein laminin. We show that most clinical isolates bind laminin and that both Hap and PE are crucial for the NTHi-dependent interaction with laminin as revealed with different mutants. The laminin-binding region is located at the N-terminus of PE, and PE binds to the heparin-binding C-terminal globular domain of laminin. PE simultaneously attracts vitronectin and laminin at separate binding sites, proving the multifunctional nature of the adhesin. This previously unknown PE-dependent interaction with laminin may contribute to NTHi colonization, particularly in smokers with COPD. |
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