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Haemophilus influenzae stores and distributes hemin by using Protein E.

Tamim, Al-Jubair LU ; Singh, Birendra LU ; Fleury, Christophe LU ; Blom, Anna LU ; Mörgelin, Matthias LU ; Thunnissen, Marjolein and Riesbeck, Kristian LU (2014) In International Journal of Medical Microbiology 304(5-6). p.662-668
Abstract
The human pathogen Haemophilus influenzae causes mainly respiratory tract infections such as acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease. We recently revealed the crystal structure of H. influenzeae protein E (PE), a multifunctional adhesin that is involved in direct interactions with lung epithelial cells and host proteins. Based upon the PE structure we here suggest a hypothetical binding pocket that is compatible in size with a hemin molecule. An H. influenzae mutant devoid of PE bound significantly less hemin in comparison to the PE-expressing wild type counterpart. In addition, E. coli expressing PE at the surface resulted in a hemin-binding phenotype. An interaction between... (More)
The human pathogen Haemophilus influenzae causes mainly respiratory tract infections such as acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease. We recently revealed the crystal structure of H. influenzeae protein E (PE), a multifunctional adhesin that is involved in direct interactions with lung epithelial cells and host proteins. Based upon the PE structure we here suggest a hypothetical binding pocket that is compatible in size with a hemin molecule. An H. influenzae mutant devoid of PE bound significantly less hemin in comparison to the PE-expressing wild type counterpart. In addition, E. coli expressing PE at the surface resulted in a hemin-binding phenotype. An interaction between hemin and recombinant soluble PE was also demonstrated by native-PAGE and UV-visible spectrophotometry. Surface plasmon resonance revealed an affinity (Kd) of 1.6×10(-6)M for the hemin-PE interaction. Importantly, hemin that was bound to PE at the H. influenzae surface, was donated to co-cultured luciferase-expressing H. influenzae that were starved of hemin. When hemin is bound to PE it thus may serve as a storage pool for H. influenzae. To our knowledge this is the first report showing that H. influenzae can share hemin via a surface-located outer membrane protein. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
International Journal of Medical Microbiology
volume
304
issue
5-6
pages
662 - 668
publisher
Elsevier
external identifiers
  • pmid:24863527
  • wos:000339775600018
  • scopus:84903819516
ISSN
1618-0607
DOI
10.1016/j.ijmm.2014.04.015
language
English
LU publication?
yes
id
922189ac-615f-47f4-864e-1259f3366bdf (old id 4452542)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/24863527?dopt=Abstract
date added to LUP
2014-06-06 20:54:05
date last changed
2017-01-01 03:49:18
@article{922189ac-615f-47f4-864e-1259f3366bdf,
  abstract     = {The human pathogen Haemophilus influenzae causes mainly respiratory tract infections such as acute otitis media in children and exacerbations in patients with chronic obstructive pulmonary disease. We recently revealed the crystal structure of H. influenzeae protein E (PE), a multifunctional adhesin that is involved in direct interactions with lung epithelial cells and host proteins. Based upon the PE structure we here suggest a hypothetical binding pocket that is compatible in size with a hemin molecule. An H. influenzae mutant devoid of PE bound significantly less hemin in comparison to the PE-expressing wild type counterpart. In addition, E. coli expressing PE at the surface resulted in a hemin-binding phenotype. An interaction between hemin and recombinant soluble PE was also demonstrated by native-PAGE and UV-visible spectrophotometry. Surface plasmon resonance revealed an affinity (Kd) of 1.6×10(-6)M for the hemin-PE interaction. Importantly, hemin that was bound to PE at the H. influenzae surface, was donated to co-cultured luciferase-expressing H. influenzae that were starved of hemin. When hemin is bound to PE it thus may serve as a storage pool for H. influenzae. To our knowledge this is the first report showing that H. influenzae can share hemin via a surface-located outer membrane protein.},
  author       = {Tamim, Al-Jubair and Singh, Birendra and Fleury, Christophe and Blom, Anna and Mörgelin, Matthias and Thunnissen, Marjolein and Riesbeck, Kristian},
  issn         = {1618-0607},
  language     = {eng},
  number       = {5-6},
  pages        = {662--668},
  publisher    = {Elsevier},
  series       = {International Journal of Medical Microbiology},
  title        = {Haemophilus influenzae stores and distributes hemin by using Protein E.},
  url          = {http://dx.doi.org/10.1016/j.ijmm.2014.04.015},
  volume       = {304},
  year         = {2014},
}