Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter
Singh, Birendra LU ; Jubair, Tamim Al LU ; Mörgelin, Matthias LU ; Sundin, Anders LU ; Linse, Sara LU ; Nilsson, Ulf J. LU and Riesbeck, Kristian LU
(2015)
In International Journal of Medical Microbiology
305(1).
p.27-37
- Abstract
The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100. nm long fibril at the bacterial surface albeit the length is approximately 200. nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl... (More)
The Haemophilus surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated Haemophilus influenzae. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100. nm long fibril at the bacterial surface albeit the length is approximately 200. nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl unfolded the Hsf molecules, and resulted in an increased length of fibres in comparison to the native trimeric form. Importantly, our findings were also verified by E. coli expressing Hsf at its surface. In addition, a set of Hsf-specific peptide antibodies also indicated that the N-terminal of Hsf is located near the C-terminal at the base of the fibril. Taken together, our results demonstrated that Hsf is not a straight molecule but is folded and doubled over. This is the first report that provides the unique structural features of the trimeric autotransporter Hsf.
(Less)
- author
- Singh, Birendra
LU
; Jubair, Tamim Al
LU
; Mörgelin, Matthias
LU
; Sundin, Anders
LU
; Linse, Sara
LU
; Nilsson, Ulf J.
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Haemophilus influenzae type b, Haemophilus surface fibril, Hib, Hsf
- in
- International Journal of Medical Microbiology
- volume
- 305
- issue
- 1
- pages
- 11 pages
- publisher
- Elsevier
- external identifiers
-
- pmid:25465160
- wos:000348957700004
- pmid:25465160
- scopus:84940163417
- ISSN
- 1618-0607
- DOI
- 10.1016/j.ijmm.2014.10.004
- language
- English
- LU publication?
- yes
- id
- f93a715d-cb14-442d-bfa8-539bfc8a8846 (old id 4912873)
- date added to LUP
- 2016-04-01 10:47:23
- date last changed
- 2023-10-19 15:45:48
@article{f93a715d-cb14-442d-bfa8-539bfc8a8846,
abstract = {{<p>The <i>Haemophilus</i> surface fibril (Hsf) is an extraordinary large (2413 amino acids) trimeric autotransporter, present in all encapsulated <i>Haemophilus influenzae</i>. It contributes to virulence by directly functioning as an adhesin. Furthermore, Hsf recruits the host factor vitronectin thereby inhibiting the host innate immune response resulting in enhanced survival in serum. Here we observed by electron microscopy that Hsf appears as an 100. nm long fibril at the bacterial surface albeit the length is approximately 200. nm according to a bioinformatics based model. To unveil this discrepancy, we denaturated Hsf at the surface of Hib by using guanidine hydrochloride (GuHCl). Partial denaturation induced in the presence of GuHCl unfolded the Hsf molecules, and resulted in an increased length of fibres in comparison to the native trimeric form. Importantly, our findings were also verified by <i>E. coli</i> expressing Hsf at its surface. In addition, a set of Hsf-specific peptide antibodies also indicated that the N-terminal of Hsf is located near the C-terminal at the base of the fibril. Taken together, our results demonstrated that Hsf is not a straight molecule but is folded and doubled over. This is the first report that provides the unique structural features of the trimeric autotransporter Hsf.</p>}},
author = {{Singh, Birendra and Jubair, Tamim Al and Mörgelin, Matthias and Sundin, Anders and Linse, Sara and Nilsson, Ulf J. and Riesbeck, Kristian}},
issn = {{1618-0607}},
keywords = {{Haemophilus influenzae type b; Haemophilus surface fibril; Hib; Hsf}},
language = {{eng}},
number = {{1}},
pages = {{27--37}},
publisher = {{Elsevier}},
series = {{International Journal of Medical Microbiology}},
title = {{Haemophilus influenzae surface fibril (Hsf) is a unique twisted hairpin-like trimeric autotransporter}},
url = {{https://lup.lub.lu.se/search/files/2137927/7752889.pdf}},
doi = {{10.1016/j.ijmm.2014.10.004}},
volume = {{305}},
year = {{2015}},
}