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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1035418
- author
- Ronander, Elena
LU
; Brant, Marta
LU
; Janson, Håkan
LU
; Sheldon, Joanna
; Forsgren, Arne
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2008
- 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
- pmid:18069033
- 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
- 2016-04-01 11:45:03
- date last changed
- 2025-10-14 11:11:02
@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}},
doi = {{10.1016/j.micinf.2007.10.006}},
volume = {{10}},
year = {{2008}},
}