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Haemophilus influenzae Protein E Binds to the Extracellular Matrix by Concurrently Interacting With Laminin and Vitronectin

Hallstrom, Teresia; Singh, Birendra LU ; Resman, Fredrik; Blom, Anna LU ; Mörgelin, Matthias LU and Riesbeck, Kristian LU (2011) In Journal of Infectious Diseases 204(7). p.1065-1074
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... (More)
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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Infectious Diseases
volume
204
issue
7
pages
1065 - 1074
publisher
Oxford University Press
external identifiers
  • wos:000294595900014
  • scopus:80052404108
ISSN
1537-6613
DOI
10.1093/infdis/jir459
language
English
LU publication?
yes
id
cd9a19e9-cdea-4218-9c0c-8c987d7c76f4 (old id 2186849)
date added to LUP
2011-11-01 07:52:28
date last changed
2017-07-30 04:05:05
@article{cd9a19e9-cdea-4218-9c0c-8c987d7c76f4,
  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.},
  author       = {Hallstrom, Teresia and Singh, Birendra and Resman, Fredrik and Blom, Anna and Mörgelin, Matthias and Riesbeck, Kristian},
  issn         = {1537-6613},
  language     = {eng},
  number       = {7},
  pages        = {1065--1074},
  publisher    = {Oxford University Press},
  series       = {Journal of Infectious Diseases},
  title        = {Haemophilus influenzae Protein E Binds to the Extracellular Matrix by Concurrently Interacting With Laminin and Vitronectin},
  url          = {http://dx.doi.org/10.1093/infdis/jir459},
  volume       = {204},
  year         = {2011},
}