A new Factor Xa inhibitor from Amblyomma cajennense with a unique domain composition

Arch Biochem Biophys. 2010 Jan 15;493(2):151-6. doi: 10.1016/j.abb.2009.10.009. Epub 2009 Oct 22.

Abstract

Bioactive compounds of great interest are found in the saliva of hematophagous organisms. While exploring a cDNA library derived from the salivary glands of the tick Amblyomma cajennense, a transcript that codes for a protein with unique structure (containing an N-terminal Kunitz-type domain and a C-terminus with no homology to any annotated sequences) was found. The recombinant mature form of this protein ( approximately 13.5kDa) was produced in Escherichia coli BL21 (DE3), and it was able to inhibit Factor Xa (FXa) and extend global blood clotting times in vitro and ex vivo. Static and dynamic predictions of its tertiary structure indicate regions that may be related to its FXa inhibitor function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Factor Xa / chemistry*
  • Factor Xa / metabolism
  • Factor Xa Inhibitors*
  • Humans
  • Ixodidae / chemistry*
  • Ixodidae / genetics
  • Ixodidae / metabolism
  • Protein Structure, Tertiary / physiology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Serine Proteinase Inhibitors / chemistry*
  • Serine Proteinase Inhibitors / genetics
  • Serine Proteinase Inhibitors / metabolism
  • Structure-Activity Relationship

Substances

  • DNA, Complementary
  • Factor Xa Inhibitors
  • Recombinant Proteins
  • Serine Proteinase Inhibitors
  • Factor Xa