Advanced

The crystal structure of PD1, a Haemophilus surface fibril domain

Wright, Jack; Thomsen, Maren; Kolodziejczyk, Robert; Ridley, Joshua; Sinclair, Jessica; Carrington, Glenn; Singh, Birendra LU ; Riesbeck, Kristian LU and Goldman, Adrian (2017) In Acta crystallographica. Section F, Structural biology communications 73(2). p.101-108
Abstract

The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel 'hairpin like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 Å resolution. The structure corrects the previous domain annotation by revealing the presence of an... (More)

The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel 'hairpin like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 Å resolution. The structure corrects the previous domain annotation by revealing the presence of an unexpected N terminal TrpRing domain. PD1 represents the first Hsf domain to be solved, and thus paves the way for further research on the 'hairpin like' hypothesis.

(Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
adhesin, cell adhesion, Haemophilus influenzae, Haemophilus surface fibril, Hsf putative domain 1, trimeric autotransporter
in
Acta crystallographica. Section F, Structural biology communications
volume
73
issue
2
pages
8 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:85011967818
  • wos:000396915200007
ISSN
2053-230X
DOI
10.1107/S2053230X17001406
language
English
LU publication?
yes
id
cfa988a7-e715-4164-adf2-e51e03857c00
date added to LUP
2017-02-23 10:04:39
date last changed
2018-01-07 11:52:13
@article{cfa988a7-e715-4164-adf2-e51e03857c00,
  abstract     = {<p>The Haemophilus surface fibril (Hsf) is an unusually large trimeric autotransporter adhesin (TAA) expressed by the most virulent strains of H. influenzae. Hsf is known to mediate adhesion between pathogen and host, allowing the establishment of potentially deadly diseases such as epiglottitis, meningitis and pneumonia. While recent research has suggested that this TAA might adopt a novel 'hairpin like' architecture, the characterization of Hsf has been limited to in silico modelling and electron micrographs, with no high resolution structural data available. Here, the crystal structure of Hsf putative domain 1 (PD1) is reported at 3.3 Å resolution. The structure corrects the previous domain annotation by revealing the presence of an unexpected N terminal TrpRing domain. PD1 represents the first Hsf domain to be solved, and thus paves the way for further research on the 'hairpin like' hypothesis.</p>},
  author       = {Wright, Jack and Thomsen, Maren and Kolodziejczyk, Robert and Ridley, Joshua and Sinclair, Jessica and Carrington, Glenn and Singh, Birendra and Riesbeck, Kristian and Goldman, Adrian},
  issn         = {2053-230X},
  keyword      = {adhesin,cell adhesion,Haemophilus influenzae,Haemophilus surface fibril,Hsf putative domain 1,trimeric autotransporter},
  language     = {eng},
  month        = {02},
  number       = {2},
  pages        = {101--108},
  publisher    = {Wiley-Blackwell},
  series       = {Acta crystallographica. Section F, Structural biology communications},
  title        = {The crystal structure of PD1, a Haemophilus surface fibril domain},
  url          = {http://dx.doi.org/10.1107/S2053230X17001406},
  volume       = {73},
  year         = {2017},
}