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Identification of a novel Haemophilus influenzae protein important for adhesion to epithelial cells.

Ronander, Elena LU ; Brant, Marta LU ; Janson, Håkan LU ; Sheldon, Joanna; Forsgren, Arne LU and Riesbeck, Kristian LU (2008) In Microbes and Infection 10(1). p.87-96
Abstract
Non-typable Haemophilus influenzae (NTHi) is an important human-specific respiratory pathogen colonizing the mucosa of the upper respiratory tract. The bacterium is a common cause of acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease (COPD). An immunoglobulin (Ig) D-lambda myeloma protein was found to detect a 16kDa surface protein that we designated protein E (PE). The pe gene was cloned using an NTHi genomic DNA library, and a truncated PE-derived protein lacking the endogenous signal peptide (PE22-160) was synthesized and produced in large amounts in Escherichia coli. Interestingly, PE was expressed at the bacterial surface of NTHi as revealed by flow cytometry using the IgD-lambda... (More)
Non-typable Haemophilus influenzae (NTHi) is an important human-specific respiratory pathogen colonizing the mucosa of the upper respiratory tract. The bacterium is a common cause of acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease (COPD). An immunoglobulin (Ig) D-lambda myeloma protein was found to detect a 16kDa surface protein that we designated protein E (PE). The pe gene was cloned using an NTHi genomic DNA library, and a truncated PE-derived protein lacking the endogenous signal peptide (PE22-160) was synthesized and produced in large amounts in Escherichia coli. Interestingly, PE was expressed at the bacterial surface of NTHi as revealed by flow cytometry using the IgD-lambda myeloma protein or PE-specific polyclonal antibodies. A PE-deficient NTHi mutant was produced and lost 50% of its adhesive capacity as compared to the wild-type counterpart when analysed for adhesion to type II lung alveolar epithelial cells. In parallel, E. coli expressing full-length PE1-160 adhered significantly more efficiently to epithelial cells as compared to wild-type E. coli. Recombinant IgD that recognized the chemical dansyl-chloride did not interact with PE indicating that the IgD-lambda myeloma protein most likely was an antibody directed against the H. influenzae surface epitope. In conclusion, we have discovered a novel NTHi outer membrane protein with adhesive properties using an IgD-myeloma protein. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Microbes and Infection
volume
10
issue
1
pages
87 - 96
publisher
Elsevier
external identifiers
  • pmid:18069033
  • wos:000254372500013
  • scopus:39049089536
ISSN
1769-714X
DOI
10.1016/j.micinf.2007.10.006
language
English
LU publication?
yes
id
1e1e2a02-f1dd-4664-a16e-92da9d67526b (old id 1035418)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18069033?dopt=Abstract
date added to LUP
2008-08-01 14:56:09
date last changed
2017-07-30 03:34:36
@article{1e1e2a02-f1dd-4664-a16e-92da9d67526b,
  abstract     = {Non-typable Haemophilus influenzae (NTHi) is an important human-specific respiratory pathogen colonizing the mucosa of the upper respiratory tract. The bacterium is a common cause of acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease (COPD). An immunoglobulin (Ig) D-lambda myeloma protein was found to detect a 16kDa surface protein that we designated protein E (PE). The pe gene was cloned using an NTHi genomic DNA library, and a truncated PE-derived protein lacking the endogenous signal peptide (PE22-160) was synthesized and produced in large amounts in Escherichia coli. Interestingly, PE was expressed at the bacterial surface of NTHi as revealed by flow cytometry using the IgD-lambda myeloma protein or PE-specific polyclonal antibodies. A PE-deficient NTHi mutant was produced and lost 50% of its adhesive capacity as compared to the wild-type counterpart when analysed for adhesion to type II lung alveolar epithelial cells. In parallel, E. coli expressing full-length PE1-160 adhered significantly more efficiently to epithelial cells as compared to wild-type E. coli. Recombinant IgD that recognized the chemical dansyl-chloride did not interact with PE indicating that the IgD-lambda myeloma protein most likely was an antibody directed against the H. influenzae surface epitope. In conclusion, we have discovered a novel NTHi outer membrane protein with adhesive properties using an IgD-myeloma protein.},
  author       = {Ronander, Elena and Brant, Marta and Janson, Håkan and Sheldon, Joanna and Forsgren, Arne and Riesbeck, Kristian},
  issn         = {1769-714X},
  language     = {eng},
  number       = {1},
  pages        = {87--96},
  publisher    = {Elsevier},
  series       = {Microbes and Infection},
  title        = {Identification of a novel Haemophilus influenzae protein important for adhesion to epithelial cells.},
  url          = {http://dx.doi.org/10.1016/j.micinf.2007.10.006},
  volume       = {10},
  year         = {2008},
}