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Venom Components Acting on the Hemostatic System: Structural and Mechanistic Insights

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A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".

Deadline for manuscript submissions: 20 May 2024 | Viewed by 4432

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Special Issue Editors

Dr. Russolina Benedeta Zingali

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Guest Editor

Laboratório de Hemostase e Venenos, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil
Interests: structure–activity relationship; proteomics; hemostasis; cancer; snake venom treatment

Dr. Robson Monteiro

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Guest Editor

Laboratório de Trombose, Câncer e Inflamação, Instituto de Bioquímica Médica Leopoldo de Meis, Universidade Federal do Rio de Janeiro, Rio de Janeiro 21.941-902, Brazil
Interests: cancer; thrombosis; inflammation

Special Issue Information

Dear Colleagues,

Venoms from different species of animals contain components, mainly proteins, and peptides, that can interfere with various physiopathological processes, including cancer, inflammation, neurotransmission, immune responses, cell growth, apoptosis, hemostasis, and others. The effects of crude venom from snakes on hemostasis have been recorded since the late 1700s. A large variety of molecules that interfere in the hemostatic process have been isolated, and their mechanisms of action characterized. For instance, molecules that perturb the hemostatic system can display pro or anticoagulant effects, activate or inhibit platelet aggregation, interfere in clot dissolution, and interfere with endothelial cells. This Special Issue focuses on the structural–activity relationship of some of these molecules and points to their mechanism of action.

Moreover, the applications of these molecules and derived analogs as tools for investigation, diagnosis, or use in drugs will also be presented and discussed.

Dr. Russolina Benedeta Zingali
Dr. Robson Monteiro
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a double-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Toxins is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

hemostasis
platelet
blood clotting
structure
mechanism of action
venom proteins
venom peptides
toxins
drug development
tools for diagnosis

Published Papers (4 papers)

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Research

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17 pages, 5158 KiB

Open AccessArticle

Isolation and Functional Characterization of Erythrofibrase: An Alfa-Fibrinogenase Enzyme from Trimeresurus erythrurus Venom of North-East India

by Susmita Thakur, Rafika Yasmin, Anita Malhotra, Hmar Tlawmte Lalremsanga, Vishal Santra, Surajit Giri and Robin Doley

Toxins 2024, 16(4), 201; https://doi.org/10.3390/toxins16040201 - 22 Apr 2024

Viewed by 384

Abstract

Green pit viper bites induce mild toxicity with painful local swelling, blistering, cellulitis, necrosis, ecchymosis and consumptive coagulopathy. Several bite cases of green pit vipers have been reported in several south-east Asian countries including the north-eastern region of India. The present study describes isolation and characterization of a haemostatically active protein from Trimeresurus erythrurus venom responsible for coagulopathy. Using a two-step chromatographic method, a snake venom serine protease erythrofibrase was purified to homogeneity. SDS-PAGE of erythrofibrase showed a single band of ~30 kDa in both reducing and non-reducing conditions. The primary structure of erythrofibrase was determined by ESI LC-MS/MS, and the partial sequence obtained showed 77% sequence similarity with other snake venom thrombin-like enzymes (SVTLEs). The partial sequence obtained had the typical 12 conserved cysteine residues, as well as the active site residues (His57, Asp102 and Ser195). Functionally, erythrofibrase showed direct fibrinogenolytic activity by degrading the Aα chain of bovine fibrinogen at a slow rate, which might be responsible for causing hypofibrinogenemia and incoagulable blood for several days in envenomated patients. Moreover, the inability of Indian polyvalent antivenom (manufactured by Premium Serum Pvt. Ltd., Maharashtra, India) to neutralize the thrombin-like and plasmin-like activity of erythrofibrase can be correlated with the clinical inefficacy of antivenom therapy. This is the first study reporting an α-fibrinogenase enzyme erythrofibrase from T. erythrurus venom, which is crucial for the pathophysiological manifestations observed in envenomated victims. Full article

(This article belongs to the Special Issue Venom Components Acting on the Hemostatic System: Structural and Mechanistic Insights)

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21 pages, 2990 KiB

Open AccessArticle

Analytical Size Exclusion Chromatography Coupled with Mass Spectrometry in Parallel with High-Throughput Venomics and Bioassaying for Venom Profiling

by Sedef Terzioglu, Mátyás A. Bittenbinder, Julien Slagboom, Bas van de Velde, Nicholas R. Casewell and Jeroen Kool

Toxins 2023, 15(9), 552; https://doi.org/10.3390/toxins15090552 - 05 Sep 2023

Cited by 1 | Viewed by 1283

Abstract

Modern analytical size exclusion chromatography (SEC) is a suitable technique to separate venom toxin families according to their size characteristics. In this study, a method was developed to separate intact venom toxins from Bungarus multicinctus and Daboia russelii venoms via analytical SEC using volatile, non-salt-containing eluents for post-column mass spectrometry, coagulation bioassaying and high-throughput venomics. Two venoms were used to demonstrate the method developed. While the venom of Bungaurs multicinctus is known to exert anticoagulant effects on plasma, in this study, we showed the existence of both procoagulant toxins and anticoagulant toxins. For Daboia russelii venom, the method revealed characteristic procoagulant effects, with a 90 kDa mass toxin detected and matched with the Factor X-activating procoagulant heterotrimeric glycoprotein named RVV-X. The strong procoagulant effects for this toxin show that it was most likely eluted from size exclusion chromatography non-denatured. In conclusion, the separation of snake venom by size gave the opportunity to separate some specific toxin families from each other non-denatured, test these for functional bioactivities, detect the eluting mass on-line via mass spectrometry and identify the eluted toxins using high-throughput venomics. Full article

(This article belongs to the Special Issue Venom Components Acting on the Hemostatic System: Structural and Mechanistic Insights)

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Review

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30 pages, 3019 KiB

Open AccessReview

Potential Biotechnological Applications of Venoms from the Viperidae Family in Central America for Thrombosis

by Jorge Eduardo Chang Estrada, Taissa Nunes Guerrero, Daniel Fernando Reyes-Enríquez, Erica Santos Nardy, Roseane Guimarães Ferreira, Cristian José Ruiz Calderón, Irmgardt A. Wellmann, Kaio Murilo Monteiro Espíndola, Alejandro Ferraz do Prado, Andreimar Martins Soares, Marcos Roberto de Mattos Fontes, Marta Chagas Monteiro and Russolina Benedeta Zingali

Toxins 2024, 16(3), 142; https://doi.org/10.3390/toxins16030142 - 08 Mar 2024

Viewed by 1109

Abstract

Central America is home to one of the most abundant herpetofauna in the Americas, occupying only 7% of the continent’s total area. Vipers and lizards are among the most relevant venomous animals in medical practice due to the consequences of envenomation from the bite of these animals. A great diversity of biomolecules with immense therapeutic and biotechnological value is contained in their venom. This paper describes the prominent leading representatives of the family Viperidae, emphasizing their morphology, distribution, habitat, feeding, and venom composition, as well as the biotechnological application of some isolated components from the venom of the animals from these families, focusing on molecules with potential anti-thrombotic action. We present the leading protein families that interfere with blood clotting, platelet activity, or the endothelium pro-thrombotic profile. In conclusion, Central America is an endemic region of venomous animals that can provide many molecules for biotechnological applications. Full article

(This article belongs to the Special Issue Venom Components Acting on the Hemostatic System: Structural and Mechanistic Insights)

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15 pages, 1430 KiB

Open AccessReview

The Role of Snake Venom Disintegrins in Angiogenesis

by Patricia Bianca Clissa, Maisa Splendore Della-Casa, Bianca Cestari Zychar and Sabri Saeed Sanabani

Toxins 2024, 16(3), 127; https://doi.org/10.3390/toxins16030127 - 01 Mar 2024

Viewed by 1139

Abstract

Angiogenesis, the formation of new blood vessels, plays a critical role in various physiological and pathological conditions. Snake venom disintegrins (SVDs) have been identified as significant regulators of this process. In this review, we explore the dual roles of SVD in angiogenesis, both as antiangiogenic agents by inhibiting integrin binding and interfering with vascular endothelial growth factors and as proangiogenic agents by enhancing integrin binding, stimulating cell migration and proliferation, and inducing neoangiogenesis. Studies in vitro and in animal models have demonstrated these effects and offer significant therapeutic opportunities. The potential applications of SVD in diseases related to angiogenesis, such as cancer, ocular diseases, tissue regeneration, wound healing, and cardiovascular diseases, are also discussed. Overall, SVDs are promising potential therapeutics, and further advances in this field could lead to innovative treatments for diseases related to angiogenesis. Full article

(This article belongs to the Special Issue Venom Components Acting on the Hemostatic System: Structural and Mechanistic Insights)

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