A fine-tuned interaction between the trimeric autotransporter Haemophilus surface fibrils and vitronectin leads to serum resistance and adherence to respiratory epithelial cells.
Singh, Birendra LU ; Su, Shanice YC LU ; Tamim, Al-Jubair LU ; Mukherjee, Oindrilla LU ; Hallström, Teresia LU ; Mörgelin, Matthias LU ; Blom, Anna LU
and Riesbeck, Kristian
LU
(2014)
In Infection and Immunity
82(6).
p.2378-2389
- Abstract
- Haemophilus influenzae type b (Hib) escapes the host immune system by recruitment of the complement regulator vitronectin that inhibits the formation of the membrane attack complex (MAC) by inhibiting C5b-C7 complex formation and C9 polymerization. We previously reported that Hib acquires vitronectin at the surface by using Haemophilus surface fibrils (Hsf). Here we studied in detail the interaction between Hsf and vitronectin and its role in inhibition of MAC formation and invasion of lung epithelial cells. The vitronectin-binding region of Hsf was defined at the N-terminal comprising amino acids Hsf 429-652. Moreover, the Hsf recognition site on vitronectin consisted of the C-terminal amino acids 352-374. H. influenzae was killed more... (More)
- Haemophilus influenzae type b (Hib) escapes the host immune system by recruitment of the complement regulator vitronectin that inhibits the formation of the membrane attack complex (MAC) by inhibiting C5b-C7 complex formation and C9 polymerization. We previously reported that Hib acquires vitronectin at the surface by using Haemophilus surface fibrils (Hsf). Here we studied in detail the interaction between Hsf and vitronectin and its role in inhibition of MAC formation and invasion of lung epithelial cells. The vitronectin-binding region of Hsf was defined at the N-terminal comprising amino acids Hsf 429-652. Moreover, the Hsf recognition site on vitronectin consisted of the C-terminal amino acids 352-374. H. influenzae was killed more rapidly in vitronectin-depleted serum when compared to normal human serum (NHS), and an increased MAC deposition was observed at the surface of an Hsf-deficient H. influenzae mutant. In parallel, Hsf-expressing E. coli selectively acquired vitronectin from serum that resulted in significant inhibition of the MAC. Moreover, when vitronectin was bound to Hsf an increased bacterial adherence and internalization of epithelial cells was observed. Taken together, we have defined a fine-tuned protein-protein interaction between Hsf and vitronectin that may contribute to an increased virulence of Hib. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4379767
- author
- Singh, Birendra
LU
; Su, Shanice YC
LU
; Tamim, Al-Jubair
LU
; Mukherjee, Oindrilla
LU
; Hallström, Teresia
LU
; Mörgelin, Matthias
LU
; Blom, Anna
LU
and Riesbeck, Kristian
LU
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Infection and Immunity
- volume
- 82
- issue
- 6
- pages
- 2378 - 2389
- publisher
- American Society for Microbiology
- external identifiers
-
- pmid:24664511
- wos:000336378100024
- scopus:84900418637
- pmid:24664511
- ISSN
- 1098-5522
- DOI
- 10.1128/IAI.01636-13
- language
- English
- LU publication?
- yes
- id
- 08475938-f95a-4b53-971b-08af618a4eb9 (old id 4379767)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/24664511?dopt=Abstract
- date added to LUP
- 2016-04-01 10:30:45
- date last changed
- 2022-02-25 02:27:35
@article{08475938-f95a-4b53-971b-08af618a4eb9,
abstract = {{Haemophilus influenzae type b (Hib) escapes the host immune system by recruitment of the complement regulator vitronectin that inhibits the formation of the membrane attack complex (MAC) by inhibiting C5b-C7 complex formation and C9 polymerization. We previously reported that Hib acquires vitronectin at the surface by using Haemophilus surface fibrils (Hsf). Here we studied in detail the interaction between Hsf and vitronectin and its role in inhibition of MAC formation and invasion of lung epithelial cells. The vitronectin-binding region of Hsf was defined at the N-terminal comprising amino acids Hsf 429-652. Moreover, the Hsf recognition site on vitronectin consisted of the C-terminal amino acids 352-374. H. influenzae was killed more rapidly in vitronectin-depleted serum when compared to normal human serum (NHS), and an increased MAC deposition was observed at the surface of an Hsf-deficient H. influenzae mutant. In parallel, Hsf-expressing E. coli selectively acquired vitronectin from serum that resulted in significant inhibition of the MAC. Moreover, when vitronectin was bound to Hsf an increased bacterial adherence and internalization of epithelial cells was observed. Taken together, we have defined a fine-tuned protein-protein interaction between Hsf and vitronectin that may contribute to an increased virulence of Hib.}},
author = {{Singh, Birendra and Su, Shanice YC and Tamim, Al-Jubair and Mukherjee, Oindrilla and Hallström, Teresia and Mörgelin, Matthias and Blom, Anna and Riesbeck, Kristian}},
issn = {{1098-5522}},
language = {{eng}},
number = {{6}},
pages = {{2378--2389}},
publisher = {{American Society for Microbiology}},
series = {{Infection and Immunity}},
title = {{A fine-tuned interaction between the trimeric autotransporter Haemophilus surface fibrils and vitronectin leads to serum resistance and adherence to respiratory epithelial cells.}},
url = {{http://dx.doi.org/10.1128/IAI.01636-13}},
doi = {{10.1128/IAI.01636-13}},
volume = {{82}},
year = {{2014}},
}