Active but inoperable thrombin is accumulated in a plasma protein layer surrounding Streptococcus pyogenes.
Naudin, Clément LU ; Hurley, Sinead LU ; Malmström, Erik LU ; Plug, T ; Shannon, Oonagh LU ; Meijers, J C M ; Mörgelin, Matthias LU ; Björck, Lars LU and Herwald, Heiko LU
(2015)
In Thrombosis and Haemostasis
114(4).
p.717-726
- Abstract
- Activation of thrombin is a critical determinant in many physiological and pathological processes including haemostasis and inflammation. Under physiological conditions many of these functions are involved in wound healing or eradication of an invading pathogen. However, when activated systemically, thrombin can contribute to severe and life-threatening conditions by causing complications such as multiple multi-organ failure and disseminated intravascular coagulation. In the present study we investigated how the activity of thrombin is modulated when it is bound to the surface of Streptococcus pyogenes. Our data show that S. pyogenes bacteria become covered with a proteinaceous layer when incubated with human plasma, and that thrombin is a... (More)
- Activation of thrombin is a critical determinant in many physiological and pathological processes including haemostasis and inflammation. Under physiological conditions many of these functions are involved in wound healing or eradication of an invading pathogen. However, when activated systemically, thrombin can contribute to severe and life-threatening conditions by causing complications such as multiple multi-organ failure and disseminated intravascular coagulation. In the present study we investigated how the activity of thrombin is modulated when it is bound to the surface of Streptococcus pyogenes. Our data show that S. pyogenes bacteria become covered with a proteinaceous layer when incubated with human plasma, and that thrombin is a constituent of this layer. Though the coagulation factor is found attached to the bacteria with a functional active site, thrombin has lost its capacity to interact with its natural substrates and inhibitors. Thus, the interaction of bacteria with human plasma renders thrombin completely inoperable at the streptococcal surface. This could represent a host defense mechanism to avoid systemic activation of coagulation which could be otherwise induced when bacteria enter the circulation and cause systemic infection. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5448402
- author
- Naudin, Clément
LU
; Hurley, Sinead
LU
; Malmström, Erik
LU
; Plug, T
; Shannon, Oonagh
LU
; Meijers, J C M
; Mörgelin, Matthias
LU
; Björck, Lars
LU
and Herwald, Heiko
LU
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Thrombosis and Haemostasis
- volume
- 114
- issue
- 4
- pages
- 717 - 726
- publisher
- Schattauer GmbH
- external identifiers
-
- pmid:25994766
- wos:000362144300009
- scopus:84943169549
- pmid:25994766
- ISSN
- 0340-6245
- DOI
- 10.1160/TH15-02-0127
- project
- Contact system project
- language
- English
- LU publication?
- yes
- id
- bd3968ca-6a2a-43db-b5ca-6da61577885b (old id 5448402)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/25994766?dopt=Abstract
- date added to LUP
- 2016-04-01 15:04:32
- date last changed
- 2022-04-14 21:13:44
@article{bd3968ca-6a2a-43db-b5ca-6da61577885b,
abstract = {{Activation of thrombin is a critical determinant in many physiological and pathological processes including haemostasis and inflammation. Under physiological conditions many of these functions are involved in wound healing or eradication of an invading pathogen. However, when activated systemically, thrombin can contribute to severe and life-threatening conditions by causing complications such as multiple multi-organ failure and disseminated intravascular coagulation. In the present study we investigated how the activity of thrombin is modulated when it is bound to the surface of Streptococcus pyogenes. Our data show that S. pyogenes bacteria become covered with a proteinaceous layer when incubated with human plasma, and that thrombin is a constituent of this layer. Though the coagulation factor is found attached to the bacteria with a functional active site, thrombin has lost its capacity to interact with its natural substrates and inhibitors. Thus, the interaction of bacteria with human plasma renders thrombin completely inoperable at the streptococcal surface. This could represent a host defense mechanism to avoid systemic activation of coagulation which could be otherwise induced when bacteria enter the circulation and cause systemic infection.}},
author = {{Naudin, Clément and Hurley, Sinead and Malmström, Erik and Plug, T and Shannon, Oonagh and Meijers, J C M and Mörgelin, Matthias and Björck, Lars and Herwald, Heiko}},
issn = {{0340-6245}},
language = {{eng}},
number = {{4}},
pages = {{717--726}},
publisher = {{Schattauer GmbH}},
series = {{Thrombosis and Haemostasis}},
title = {{Active but inoperable thrombin is accumulated in a plasma protein layer surrounding Streptococcus pyogenes.}},
url = {{http://dx.doi.org/10.1160/TH15-02-0127}},
doi = {{10.1160/TH15-02-0127}},
volume = {{114}},
year = {{2015}},
}