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Haemophilus influenzae Protein F Mediates Binding to Laminin and Human Pulmonary Epithelial Cells.

Jalalvand, Farshid LU ; Su, Yu-Ching; Mörgelin, Matthias LU ; Brant, Marta LU ; Hallgren, Oskar LU ; Westergren-Thorsson, Gunilla LU ; Singh, Birendra LU and Riesbeck, Kristian LU (2012) In Journal of Infectious Diseases
Abstract
The mucosal pathogen non-typeable Haemophilus influenzae (NTHi) adheres to the respiratory epithelium, or in the case of epithelial damage, to the underlying basement membrane and extracellular matrix that amongst other proteins consists of laminin. We have recently identified Protein F, an ABC-transporter involved in NTHi immune evasion. Homology modeling of the Protein F tertiary structure revealed a strong resemblance to the streptococcal laminin-binding proteins Lbp and Lmb. Here, we show that Protein F promotes binding of NTHi to laminin and primary bronchial epithelial cells. Analyses with recombinant proteins and synthetic peptides revealed that the N-terminal part of Protein F contains the host-interacting region. Moreover, Protein... (More)
The mucosal pathogen non-typeable Haemophilus influenzae (NTHi) adheres to the respiratory epithelium, or in the case of epithelial damage, to the underlying basement membrane and extracellular matrix that amongst other proteins consists of laminin. We have recently identified Protein F, an ABC-transporter involved in NTHi immune evasion. Homology modeling of the Protein F tertiary structure revealed a strong resemblance to the streptococcal laminin-binding proteins Lbp and Lmb. Here, we show that Protein F promotes binding of NTHi to laminin and primary bronchial epithelial cells. Analyses with recombinant proteins and synthetic peptides revealed that the N-terminal part of Protein F contains the host-interacting region. Moreover, Protein F exists in all clinical isolates, and isogenic NTHi Δhpf mutants display significantly reduced binding to laminin and epithelial cells. We thus suggest Protein F as an important and ubiquitous NTHi adhesin. (Less)
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Contribution to journal
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published
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Journal of Infectious Diseases
publisher
Oxford University Press
external identifiers
  • wos:000314894600014
  • pmid:23230060
  • scopus:84873684522
ISSN
1537-6613
DOI
10.1093/infdis/jis754
language
English
LU publication?
yes
id
10b2a626-7c39-4109-88ca-5e897f71bc73 (old id 3347316)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/23230060?dopt=Abstract
date added to LUP
2013-01-02 15:29:18
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2017-05-28 03:56:40
@article{10b2a626-7c39-4109-88ca-5e897f71bc73,
  abstract     = {The mucosal pathogen non-typeable Haemophilus influenzae (NTHi) adheres to the respiratory epithelium, or in the case of epithelial damage, to the underlying basement membrane and extracellular matrix that amongst other proteins consists of laminin. We have recently identified Protein F, an ABC-transporter involved in NTHi immune evasion. Homology modeling of the Protein F tertiary structure revealed a strong resemblance to the streptococcal laminin-binding proteins Lbp and Lmb. Here, we show that Protein F promotes binding of NTHi to laminin and primary bronchial epithelial cells. Analyses with recombinant proteins and synthetic peptides revealed that the N-terminal part of Protein F contains the host-interacting region. Moreover, Protein F exists in all clinical isolates, and isogenic NTHi Δhpf mutants display significantly reduced binding to laminin and epithelial cells. We thus suggest Protein F as an important and ubiquitous NTHi adhesin.},
  author       = {Jalalvand, Farshid and Su, Yu-Ching and Mörgelin, Matthias and Brant, Marta and Hallgren, Oskar and Westergren-Thorsson, Gunilla and Singh, Birendra and Riesbeck, Kristian},
  issn         = {1537-6613},
  language     = {eng},
  month        = {12},
  publisher    = {Oxford University Press},
  series       = {Journal of Infectious Diseases},
  title        = {Haemophilus influenzae Protein F Mediates Binding to Laminin and Human Pulmonary Epithelial Cells.},
  url          = {http://dx.doi.org/10.1093/infdis/jis754},
  year         = {2012},
}