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Published on: November 3, 2014
CAP superfamily proteins from venomous animals: Who we are and what to do?
Qianqian Zhang1, Jiawei Xu1, Xi Zhou1
1The National & Local Joint Engineering Laboratory of Animal Peptide Drug Development, College of Life Sciences, Hunan Normal University, Changsha, Hunan 410081, China; Peptide and small molecule drug R&D plateform, Furong Laboratory, Hunan Normal University, Changsha, 410081, Hunan, China.
Abstract:
Cysteine-rich secretory proteins (CRISPs), antigen 5 (Ag5), and pathogenesis-related (PR-1) superfamily proteins (CAP superfamily proteins) are found in diverse species across the bacterial, fungal, plant, mammalian, and venomous animal kingdoms. Notably, CAP proteins are found in a remarkable range of species across the venomous animal kingdom and are present almost ubiquitously in venoms, even when venoms are produced in very small quantities. Meanwhile, in comparison to mammals, venomous animals are underappreciated and easy to ignore. Overwhelming evidence suggests that CAP proteins derived from venomous animals exhibit diverse activities, including ion channel, inflammatory, proteolysis, and immune regulatory activities. To understand the potential biological functions of CAP proteins in venom more effectively, we need to examine the significance of the evolution of venomous animals in the animal kingdom, for their survival. In this article, we will review the current status of research on CAP proteins in venomous animals, including their isolation, characterization, known biological activities, and sequence alignments. We will also discuss the rapid evolution of CAP proteins with varied subtypes in venomous animals. A treasure trove of information can be obtained by studying the CAP proteins in venomous animals; hence, it is necessary to explore these proteins further.
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