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Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily

1
Faculty of Pharmaceutical Sciences, Hokkaido University, Faculty of Pharmaceutical Sciences, Hokkaido University, Kita-12, Nishi-6, Kita-ku, Sapporo 060-0812, Japan
2
Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore
3
Department of Chemistry, Faculty of Science, Fukuoka University, 19-1, 8-chomeNanakuma, Jonan-ku, Fukuoka 814-0180, Japan
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(3), 175; https://doi.org/10.3390/toxins12030175
Received: 17 February 2020 / Revised: 10 March 2020 / Accepted: 10 March 2020 / Published: 12 March 2020
The CAP protein superfamily (Cysteine-rich secretory proteins (CRISPs), Antigen 5 (Ag5), and Pathogenesis-related 1 (PR-1) proteins) is widely distributed, but for toxinologists, snake venom CRISPs are the most familiar members. Although CRISPs are found in the majority of venoms, very few of these proteins have been functionally characterized, but those that have been exhibit diverse activities. Snake venom CRISPs (svCRISPs) inhibit ion channels and the growth of new blood vessels (angiogenesis). They also increase vascular permeability and promote inflammatory responses (leukocyte and neutrophil infiltration). Interestingly, CRISPs in lamprey buccal gland secretions also manifest some of these activities, suggesting an evolutionarily conserved function. As we strive to better understand the functions that CRISPs serve in venoms, it is worth considering the broad range of CRISP physiological activities throughout the animal kingdom. In this review, we summarize those activities, known crystal structures and sequence alignments, and we discuss predicted functional sites. CRISPs may not be lethal or major components of venoms, but given their almost ubiquitous occurrence in venoms and the accelerated evolution of svCRISP genes, these venom proteins are likely to have functions worth investigating. View Full-Text
Keywords: CAP superfamily; ion channel blockage; salivary component; co-factors CAP superfamily; ion channel blockage; salivary component; co-factors
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Tadokoro, T.; M. Modahl, C.; Maenaka, K.; Aoki-Shioi, N. Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily. Toxins 2020, 12, 175.

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