Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.

The complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine pr...

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Main Authors: Anders Krarup, Russell Wallis, Julia S Presanis, Péter Gál, Robert B Sim
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2007-07-01
Series:PLoS ONE
Online Access:https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000623&type=printable
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author Anders Krarup
Russell Wallis
Julia S Presanis
Péter Gál
Robert B Sim
author_facet Anders Krarup
Russell Wallis
Julia S Presanis
Péter Gál
Robert B Sim
author_sort Anders Krarup
collection DOAJ
description The complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine protease 2 (MASP2), which cleaves complement proteins C2 and C4. We present a novel and alternative role of MASP2 in the innate immune system. We have shown that MASP2 is capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin. By using a truncated active form of MASP2 as well as full-length MASP2 in complex with MBL, we have shown that the thrombin generated is active and can cleave both factor XIII and fibrinogen, forming cross-linked fibrin. To explore the biological significance of these findings we showed that fibrin was covalently bound on a bacterial surface to which MBL/MASP2 complexes were bound. These findings suggest that, as has been proposed for invertebrates, limited clotting may contribute to the innate immune response.
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spelling doaj-art-3c3d9273f1bc4fbb9a2b3c380a45f8f72025-08-20T02:00:54ZengPublic Library of Science (PLoS)PLoS ONE1932-62032007-07-0127e62310.1371/journal.pone.0000623Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.Anders KrarupRussell WallisJulia S PresanisPéter GálRobert B SimThe complement system is an important immune mechanism mediating both recognition and elimination of foreign bodies. The lectin pathway is one pathway of three by which the complement system is activated. The characteristic protease of this pathway is Mannan-binding lectin (MBL)-associated serine protease 2 (MASP2), which cleaves complement proteins C2 and C4. We present a novel and alternative role of MASP2 in the innate immune system. We have shown that MASP2 is capable of promoting fibrinogen turnover by cleavage of prothrombin, generating thrombin. By using a truncated active form of MASP2 as well as full-length MASP2 in complex with MBL, we have shown that the thrombin generated is active and can cleave both factor XIII and fibrinogen, forming cross-linked fibrin. To explore the biological significance of these findings we showed that fibrin was covalently bound on a bacterial surface to which MBL/MASP2 complexes were bound. These findings suggest that, as has been proposed for invertebrates, limited clotting may contribute to the innate immune response.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000623&type=printable
spellingShingle Anders Krarup
Russell Wallis
Julia S Presanis
Péter Gál
Robert B Sim
Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
PLoS ONE
title Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
title_full Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
title_fullStr Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
title_full_unstemmed Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
title_short Simultaneous activation of complement and coagulation by MBL-associated serine protease 2.
title_sort simultaneous activation of complement and coagulation by mbl associated serine protease 2
url https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0000623&type=printable
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AT petergal simultaneousactivationofcomplementandcoagulationbymblassociatedserineprotease2
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