Tick Saliva Protein Evasin-3 Allows for Visualization of Inflammation in Arteries through Interactions with CXC-Type Chemokines Deposited on Activated Endothelium

Stepan S. Denisov, Alexandra C. A. Heinzmann, Tanja Vajen, Mark H. M. Vries, Remco T. A. Megens, Dennis Suylen, Rory R. Koenen, Mark J. Post, Johannes H. Ippel, Tilman M. Hackeng, Ingrid Dijkgraaf*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

5 Citations (Web of Science)

Abstract

Atherosclerosis is one of the leading causes of mortality in developed and developing countries. The onset of atherosclerosis development is accompanied by overexpression of several inflammatory chemokines. Neutralization of these chemokines by chemokine-binding agents attenuates atherosclerosis progression. Here, we studied structural binding features of the tick protein Evasin-3 to chemokine (C-X-C motif) ligand 1 (CXCL1). We showed that Evasin-3-bound CXCL1 is unable to activate the CXCR2 receptor, but retains affinity to glycosamino-glycans. This observation was exploited to detect inflammation by visualizing a group of closely related CXC-type chemokines deposited on cell walls in human endothelial cells and murine carotid arteries by a fluorescent Evasin-3 conjugate. This work highlights the applicability of tick-derived chemokine-binding conjugates as a platform for the development of new agents for inflammation imaging.

Original languageEnglish
Pages (from-to)948-955
Number of pages8
JournalBioconjugate Chemistry
Volume31
Issue number3
DOIs
Publication statusPublished - 20 Feb 2020

Keywords

  • MONOCYTE RECRUITMENT
  • BINDING
  • ATHEROSCLEROSIS
  • NEUTROPHILS
  • EXPRESSION
  • ARREST

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