Purification of a fragment obtained by autolysis of a PIIIb-SVMP from Bothrops alternatus venom

Velde, Andrea Carolina Van de; Moritz, Milene Nóbrega de Oliveira; Santos, Patty Karina dos; Bustillo, Soledad; Rodríguez, José Carlos; Acosta, Ofelia; Biscoglio, Mirtha J.; Selistre-de-Araújo, Heloísa Sobreiro; Leiva, Laura

doi:10.1016/j.ijbiomac.2018.02.063

Cited by 8 publications

(3 citation statements)

References 35 publications

(55 reference statements)

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“…Some of these have been shown or predicted to arise from P-III SVMPs by proteolysis [7]. P-III SVMPs that autolyse in vitro to DC and MP fragments require alkaline conditions, an absence of Ca 2+ , and slightly elevated temperature [19][20][21][22][23][24][25][26][27]. However, such conditions do not exist in venom glands [7].…”

Section: Discussionmentioning

confidence: 99%

“…It is widely accepted that these are products of autoproteolytic processing of P-III SVMPs into their MP and DC parts [6]. This has relied on reports that some P-III SVMPs can be autoproteolytically processed in vitro to DC proteins [19][20][21][22][23][24][25][26][27]. Only one autoproteolytic product, acucetin, has been tested for its effects on platelets, where it was shown to inhibit platelet aggregation induced by ADP and collagen.…”

Section: Introductionmentioning

confidence: 99%

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Genomic Confirmation of the P-IIIe Subclass of Snake Venom Metalloproteinases and Characterisation of Its First Member, a Disintegrin-Like/Cysteine-Rich Protein

Požek

Leonardi

Pungerčar

et al. 2022

Toxins

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Disintegrin-like/cysteine-rich (DC) proteins have long been regarded just as products of proteolysis of P-III snake venom metalloproteinases (SVMPs). However, here we demonstrate that a DC protein from the venom of Vipera ammodytes (Vaa; nose-horned viper), VaaMPIII-3, is encoded per se by a P-III SVMP-like gene that has a deletion in the region of the catalytic metalloproteinase domain and in part of the non-catalytic disintegrin-like domain. In this way, we justify the proposal of the introduction of a new subclass P-IIIe of SVMP-derived DC proteins. We purified VaaMPIII-3 from the venom of Vaa in a series of chromatographic steps. A covalent chromatography step based on thiol-disulphide exchange revealed that VaaMPIII-3 contains an unpaired Cys residue. This was demonstrated to be Cys6 in about 90% and Cys19 in about 10% of the VaaMPIII-3 molecules. We further constructed a three-dimensional homology model of VaaMPIII-3. From this model, it is evident that both Cys6 and Cys19 can pair with Cys26, which suggests that the intramolecular thiol-disulphide exchange has a regulatory function. VaaMPIII-3 is an acidic 21-kDa monomeric glycoprotein that exists in at least six N-glycoforms, with isoelectric points ranging from pH 4.5 to 5.1. Consistent with the presence of an integrin-binding motif in its sequence, SECD, VaaMPIII-3 inhibited collagen-induced platelet aggregation. It also inhibited ADP- and arachidonic-acid-induced platelet aggregation, but not ristocetin-induced platelet agglutination and the blood coagulation cascade.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Genomic Confirmation of the P-IIIe Subclass of Snake Venom Metalloproteinases and Characterisation of Its First Member, a Disintegrin-Like/Cysteine-Rich Protein

Požek

Leonardi

Pungerčar

et al. 2022

Toxins

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“…The B. alternatus species had its peptides studied on chemotactic activities and inhibition of chemotaxis induced by a disintegrin [100], a peptide that affects the proliferation of human vascular endothelial cells [101], in addition to the fragment purification of venom from this species [102]. For the species B. moojeni, a snake that also has a wide distribution in the Brazilian territory, new bradykinin-potentiating peptides were isolated [102], as well as, the renal toxicity of the poison was detected [69] and the anti-leishmania effect [104].…”

Section: Species Investigatedmentioning

confidence: 99%

Studies about Snake Peptides: a Review about Brazilian Contribution

Assis

Bittar

Amorim

et al. 2022

Braz. arch. biol. technol.

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The peptides present in snake venoms are studied because of their properties, constitutions, mechanisms of action and pharmacological potential. Recognizing this potential, the present study reports the contributions of Brazilian researchers about snake peptides, between 1975 and July 2020. Thus, this study serves as a basis for monitoring this theme in Brazil, referring to the trends and patterns of scientific production. The results indicated a significant increase in Brazilian scientific production over the years, highlighting institutions located in São Paulo state as, the Butantan Institute and University of São Paulo. The main journal where Brazilian authors publish their research is the Toxicon Journal. Collaborative networks were identified between Brazilian institutions and among other countries with Brazil. The most investigated species are found in brazilian territory, mainly those belonging to the genus Bothrops and the species Crotalus durissus. The increase in studies about this theme in Brazil is evident, however, a gap is highlighted for states outside the southeastern region and for other venomous species.

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First report on BaltCRP, a cysteine-rich secretory protein (CRISP) from Bothrops alternatus venom: Effects on potassium channels and inflammatory processes

Bernardes

Menaldo

Zoccal

et al. 2019

International Journal of Biological Macromolecules

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Purification of a fragment obtained by autolysis of a PIIIb-SVMP from Bothrops alternatus venom

Cited by 8 publications

References 35 publications

Genomic Confirmation of the P-IIIe Subclass of Snake Venom Metalloproteinases and Characterisation of Its First Member, a Disintegrin-Like/Cysteine-Rich Protein

Genomic Confirmation of the P-IIIe Subclass of Snake Venom Metalloproteinases and Characterisation of Its First Member, a Disintegrin-Like/Cysteine-Rich Protein

Studies about Snake Peptides: a Review about Brazilian Contribution

First report on BaltCRP, a cysteine-rich secretory protein (CRISP) from Bothrops alternatus venom: Effects on potassium channels and inflammatory processes

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