Haemophilus influenzae stores and distributes hemin by using Protein E.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

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.

Detaljer

Författare
Enheter & grupper
Forskningsområden

Ämnesklassifikation (UKÄ) – OBLIGATORISK

  • Mikrobiologi inom det medicinska området
Originalspråkengelska
Sidor (från-till)662-668
TidskriftInternational Journal of Medical Microbiology
Volym304
Utgivningsnummer5-6
StatusPublished - 2014
PublikationskategoriForskning
Peer review utfördJa

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Relaterad forskningsoutput

Tamim, A-J., 2016, Lund: Lund University, Faculty of Medicine. 74 s.

Forskningsoutput: AvhandlingDoktorsavhandling (sammanläggning)

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