Horseshoe Crab Coagulogen Is an Invertebrate Protein with a Nerve Growth Factor-Like Domain

Andreas Bergner, Hans Georg Beise, Wolfram Bode, Tatsushi Muta, Sadaaki Iwanaga, Robert Delotto

Research output: Contribution to journalArticlepeer-review

40 Citations (Scopus)


The rapid clotting of the horseshoe crab hemolymph is essential for both its host defense and hemostasis. It is mediated by the clotting cascade system which consists of four serine proteinase zymogens and the clottable protein coagulogen. Coagulogen, the target protein of the cascade, is converted to an insoluble gel upon activation of the cascade, giving rise to clot formation.Thus this cascade is reminiscent of the mammalian blood coagulation leading to fibrin clot. structural analysis of coagulogen revealed a polypeptide fold and disulfide bridge pattern in the C-terminal half of the molecule very similar to nerve growth (NGF). This finding assigns coagulogen as the first structurally characterized invertebrate protein which belongs to the cystine knot super-family. The putative structural similarity of coagulogen and the Drosophila morphogen Spaetzle as well as the homology of its processing proteinases suggests a common origin of the two functionally different cascades. This would exemplify a divergent evolution of two proteinase cascades having totally different functions from common ancestors in a long history of evolution.

Original languageEnglish
Pages (from-to)283-288
Number of pages6
JournalBiological Chemistry
Issue number3-4
Publication statusPublished - 1997
Externally publishedYes


  • Coagulogen
  • Crystal structure
  • Horseshoe crab
  • Nerve growth factor

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Clinical Biochemistry


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