Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites

C-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggrav...

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Main Authors: David Braig, Tracy L. Nero, Hans-Georg Koch, Benedict Kaiser, Xiaowei Wang, Jan R. Thiele, Craig J. Morton, Johannes Zeller, Jurij Kiefer, Lawrence A. Potempa, Natalie A. Mellett, Luke A. Miles, Xiao-Jun Du, Peter J. Meikle, Markus Huber-Lang, G. Björn Stark, Michael W. Parker, Karlheinz Peter, Steffen U. Eisenhardt
Format: Article
Language:English
Published: Nature Publishing Group 2017-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms14188
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spelling doaj-128f34d5a0f648b598b01c6bc5aab5a52021-05-11T07:15:51ZengNature Publishing GroupNature Communications2041-17232017-01-018111910.1038/ncomms14188Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sitesDavid Braig0Tracy L. Nero1Hans-Georg Koch2Benedict Kaiser3Xiaowei Wang4Jan R. Thiele5Craig J. Morton6Johannes Zeller7Jurij Kiefer8Lawrence A. Potempa9Natalie A. Mellett10Luke A. Miles11Xiao-Jun Du12Peter J. Meikle13Markus Huber-Lang14G. Björn Stark15Michael W. Parker16Karlheinz Peter17Steffen U. Eisenhardt18Department of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchInstitute for Biochemistry and Molecular Biology and Spemann-Graduate School for Biology and Medicine University of Freiburg, Medical Faculty of the University of FreiburgDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgBaker IDI Heart and Diabetes InstituteDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgCollege of Pharmacy, Roosevelt UniversityBaker IDI Heart and Diabetes InstituteACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchBaker IDI Heart and Diabetes InstituteBaker IDI Heart and Diabetes InstituteDepartment of Traumatology, Hand, Plastic, and Reconstructive Surgery, Center of Surgery, University of UlmDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgACRF Rational Drug Discovery Centre, St Vincent’s Institute of Medical ResearchBaker IDI Heart and Diabetes InstituteDepartment of Plastic and Hand Surgery, University of Freiburg Medical Centre, Medical Faculty of the University of FreiburgC-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggravation of inflammation.https://doi.org/10.1038/ncomms14188
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language English
format Article
sources DOAJ
author David Braig
Tracy L. Nero
Hans-Georg Koch
Benedict Kaiser
Xiaowei Wang
Jan R. Thiele
Craig J. Morton
Johannes Zeller
Jurij Kiefer
Lawrence A. Potempa
Natalie A. Mellett
Luke A. Miles
Xiao-Jun Du
Peter J. Meikle
Markus Huber-Lang
G. Björn Stark
Michael W. Parker
Karlheinz Peter
Steffen U. Eisenhardt
spellingShingle David Braig
Tracy L. Nero
Hans-Georg Koch
Benedict Kaiser
Xiaowei Wang
Jan R. Thiele
Craig J. Morton
Johannes Zeller
Jurij Kiefer
Lawrence A. Potempa
Natalie A. Mellett
Luke A. Miles
Xiao-Jun Du
Peter J. Meikle
Markus Huber-Lang
G. Björn Stark
Michael W. Parker
Karlheinz Peter
Steffen U. Eisenhardt
Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
Nature Communications
author_facet David Braig
Tracy L. Nero
Hans-Georg Koch
Benedict Kaiser
Xiaowei Wang
Jan R. Thiele
Craig J. Morton
Johannes Zeller
Jurij Kiefer
Lawrence A. Potempa
Natalie A. Mellett
Luke A. Miles
Xiao-Jun Du
Peter J. Meikle
Markus Huber-Lang
G. Björn Stark
Michael W. Parker
Karlheinz Peter
Steffen U. Eisenhardt
author_sort David Braig
title Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_short Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_full Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_fullStr Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_full_unstemmed Transitional changes in the CRP structure lead to the exposure of proinflammatory binding sites
title_sort transitional changes in the crp structure lead to the exposure of proinflammatory binding sites
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-01-01
description C-reactive protein is a pentameric protein secreted by the liver in response to injury and infection. Here Braiget al. show that conformational changes in CRP on the surface of monocyte-derived microvesicles enable binding of complement C1q and lead to activation of the complement cascade and aggravation of inflammation.
url https://doi.org/10.1038/ncomms14188
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