The isolation and characterization of a new snake venom cysteine-rich secretory protein (svCRiSP) from the venom of the Southern Pacific rattlesnake and its effect on vascular permeability

Suntravat, Montamas; Cromer, Walter; Marquez, Jessenia; Galán, Jacob A.; Zawieja, David C.; Davies, Peter; Salazar, Emelyn; Sánchez, Elda E.

doi:10.1016/j.toxicon.2019.04.006

Cited by 20 publications

(20 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Another study reported the purification of a novel svCRISP from the venom of a Southern Pacific rattlesnake Crotalus oreganus helleri. The peptide, named Hellerin, induced a dramatic increase in blood vascular permeability in vivo and in vitro [52].…”

Section: Cysteine-rich Secretory Proteinsmentioning

confidence: 99%

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

et al. 2021

View full text Add to dashboard Cite

Cardiovascular diseases (CVDs) are considered as a major cause of death worldwide. Therefore, identifying and developing therapeutic strategies to treat and reduce the prevalence of CVDs is a major medical challenge. Several drugs used for the treatment of CVDs, such as captopril, emerged from natural products, namely snake venoms. These venoms are complex mixtures of bioactive molecules, which, among other physiological networks, target the cardiovascular system, leading to them being considered in the development and design of new drugs. In this review, we describe some snake venom molecules targeting the cardiovascular system such as phospholipase A2 (PLA2), natriuretic peptides (NPs), bradykinin-potentiating peptides (BPPs), cysteine-rich secretory proteins (CRISPs), disintegrins, fibrinolytic enzymes, and three-finger toxins (3FTXs). In addition, their molecular targets, and mechanisms of action—vasorelaxation, inhibition of platelet aggregation, cardioprotective activities—are discussed. The dissection of their biological effects at the molecular scale give insights for the development of future snake venom-derived drugs.

show abstract

Section: Cysteine-rich Secretory Proteinsmentioning

confidence: 99%

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

et al. 2021

View full text Add to dashboard Cite

show abstract

“…svCRiSPs were isolated from crude venoms using two chromatographic steps consist of reverse phase C18 (Higgins Analytical PROTO 300 C18, 250 × 4.6 mm, 5 µ m column, Higgins Analytical, Inc., Mountain View, CA) and cation-exchange (Waters Protein-Pak™ SP 5PW, 7.5 × 75 mm column, Waters Corp., Milford, MA) as previously described [8].…”

Section: Purification Of Crispsmentioning

confidence: 99%

“…Venom protein identification and sequence analysis of CRiSPs (Css-CRiSP from C. s. scutulatus, Catrox-CRiSP from C. atrox, Cada-CRiSP from C. adamanteus, Chor-CRiSP from C. horridus, and App-CRiSP from A. p. piscivorus) were performed by LC-MS/MS mass spectrometry following the protocol as described by Suntravat et al [8]. N-terminal amino acid sequences and sequences generated by MS were compared to the sequences in the GenBank database using BLASTX programs.…”

Section: Lc-ms/ms Analysis and Proteomics Data Processingmentioning

confidence: 99%

“…We have recently reported that Hellerin, a svCRiSP that we have isolated from the venom of the Southern Pacific Rattlesnake, C. oreganus helleri, increases vascular permeability in vivo and in vitro [8]. This study's objective was to investigate the biological activities of svCRiSPs isolated from the venoms of the most medically significant species of North American snakes.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Profiling of signaling pathways in human dermal blood and lymphatic endothelial cells induced by snake venom cysteine-rich secretory protein (svCRiSP) from North American snakes

Suntravat

Sánchez

Reyes

et al. 2021

Proceedings of 1st International Electronic Conference on Toxins

Self Cite

View full text Add to dashboard Cite

Snake venom Cysteine-Rich Secretory Proteins (svCRiSPs) are important components in the venom of many snake species. Little is known about the contribution that they make to the local pathophysiology of snakebite. We investigated the role of svCRiSPs from the most medically significant species of North American snakes (Crotalus atrox, C. adamanteus, C. scutulatus scutulatus, C. horridus, and Agkistrodon piscivorus), focusing on the cellular and molecular mechanisms. We evaluated the biological activities of svCRiSPs (Catrox-CRiSP, Cada-CRiSP, Css-CRiSP, Chor-CRiSP, and App-CRiSP) by using both in vitro assays on human dermal lymphatic (HDLECs) and blood (HDBECs) endothelial cells permeability and in vivo Miles assay. Of all the CRiSPs tested, Css-CRiSP and App-CRiSP displayed the highest increase in permeability compared to other crotaline CRiSPs. We initially screened the changes in protein expression and phosphorylation in HDLECs and HDBECs after treatment with Css-CRiSP and App-CRiSP using reverse phase protein arrays (RPPA). Studies are ongoing for identifying the key signaling that are involved in endothelial permeability after treatment with App-CRiSP and Css-CRiSP.

show abstract

“…The effect of hellerin, from Crotalus oreganus helleri venom, on vascular permeability was demonstrated in vivo and in vitro. Trans-capillary leakage was observed 30 min after mice were subcutaneously injected with hellerin (70 nM), but leakage was approximately half that of the vascular permeability produced by vascular endothelial growth factor A (VEGF-A, 50 nM) [64]. Hellerin (2 M) reduced the viability of HUVECs by 50%, and hellerin-treated HUVEC cells had rounded cell shapes and detached from the substrate.…”

Section: Vascular Permeability Regulatormentioning

confidence: 99%

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

Tadokoro

Modahl

Maenaka

et al. 2020

Toxins

View full text Add to dashboard Cite

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.

show abstract

The isolation and characterization of a new snake venom cysteine-rich secretory protein (svCRiSP) from the venom of the Southern Pacific rattlesnake and its effect on vascular permeability

Cited by 20 publications

References 34 publications

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases

Profiling of signaling pathways in human dermal blood and lymphatic endothelial cells induced by snake venom cysteine-rich secretory protein (svCRiSP) from North American snakes

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

Contact Info

Product

Resources

About