Nature Communications (Jan 2017)

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

  • 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

DOI
https://doi.org/10.1038/ncomms14188
Journal volume & issue
Vol. 8, no. 1
pp. 1 – 19

Abstract

Read online

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.