Nitrophorins and related antihemostatic lipocalins from Rhodnius prolixus and other blood-sucking arthropods

William R. Montfort, Andrzej Weichsel, John F. Andersen

Research output: Contribution to journalReview articlepeer-review

140 Scopus citations


Recent gene sequence and crystal structure determinations of salivary proteins from several blood-sucking arthropods have revealed an unusual evolutionary relationship: many such proteins derive their functions from lipocalin protein folds. Many blood-sucking arthropods have independently evolved the ability to overcome a host organism's means of preventing blood loss (called hemostasis). Most blood feeders have proteins that induce vasodilation, inhibit blood coagulation, and reduce inflammation, but do so by distinctly different mechanisms. Despite this diversity, in many cases the antihemostatic activities in such organisms reside in proteins with lipocalin folds. Thirteen such lipocalins are described in this review, with a particular focus on the heme-containing nitrophorins from Rhodnius prolixus, which transport nitric oxide, sequester histamine, and disrupt blood coagulation. Also described are the antiplatelet compounds RPAI, moubatin, and pallidipin from R. prolixus, Ornithodoros moubata, and Triatoma pallidipennis; the antithrombin protein triabin from T. pallidipennis; and the tick histamine binding proteins from Rhipicephalus appendiculatus. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)110-118
Number of pages9
JournalBiochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Issue number1-2
StatePublished - Oct 18 2000


  • Anticoagulant
  • Hemostasis
  • Histamine
  • Lipocalin
  • Nitric oxide
  • Platelet

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology


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