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Special Issue "Identification and Functional Characterization of Novel Venom Components"

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

Deadline for manuscript submissions: 31 January 2020.

Special Issue Editor

Guest Editor
Dr. Steven D. Aird

Division of Faculty Affairs and Ecology and Evolution Unit, Okinawa Institute of Science and Technology, 1919-1 Tancha, Onna-son, Kunigami-gun, Okinawa 904-0495, Japan
E-Mail
Interests: chemistry of animal venoms, particularly of snakes; snake envenomation strategies; contributions of individual venom components to prey immobilization; ecology of venomous animals

Special Issue Information

Dear Colleagues,

Throughout most of the 20th century, the toxinological literature consisted largely of pharmacological and functional characterizations of crude venoms and venom constituents, often constituents that could not be identified unambiguously. The advent of amino acid composition analysis in the 1950s enabled the first forays into physical characterizations of purified toxins, though these remained few in number until the 1970s. Then, tryptic and chymotryptic cleavage of venom proteins coupled with manual Edman degradation began to provide the first complete sequences, particularly of three-finger toxins. Polyacrylamide gel electrophoresis and improved resins for liquid chromatography permitted improved purification and better gross structural characterization of venom components. The early 1980s saw the advent of automated Edman degradation, and entire sequences of longer proteins began to appear in the literature. Then, the molecular biology revolution made it possible to generate cDNA sequences of more and larger proteins, followed by mass spectrometry-based proteomics and quantitative high-throughput DNA sequencing and genomics. Today, we face a hitherto unprecedented situation in which our capacity to generate sequence/structural data has completely overwhelmed our capacity to characterize venom constituents functionally.

This Special Issue of Toxins is devoted specifically to the discovery and functional characterization of novel venom constituents of vertebrate and invertebrate venoms.

Dr. Steven D. Aird
Guest Editor

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 papers will be 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 1800 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.

Published Papers (2 papers)

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Research

Open AccessArticle
The Dual α-Amidation System in Scorpion Venom Glands
Received: 4 June 2019 / Revised: 18 July 2019 / Accepted: 18 July 2019 / Published: 20 July 2019
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Abstract
Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion proproteins suggests that a conserved [...] Read more.
Many peptides in scorpion venoms are amidated at their C-termini. This post-translational modification is paramount for the correct biological function of ion channel toxins and antimicrobial peptides, among others. The discovery of canonical amidation sequences in transcriptome-derived scorpion proproteins suggests that a conserved enzymatic α-amidation system must be responsible for this modification of scorpion peptides. A transcriptomic approach was employed to identify sequences putatively encoding enzymes of the α-amidation pathway. A dual enzymatic α-amidation system was found, consisting of the membrane-anchored, bifunctional, peptidylglycine α-amidating monooxygenase (PAM) and its paralogs, soluble monofunctional peptidylglycine α-hydroxylating monooxygenase (PHMm) and peptidyl-α-hydroxyglycine α-amidating lyase (PALm). Independent genes encode these three enzymes. Amino acid residues responsible for ion coordination and enzymatic activity are conserved in these sequences, suggesting that the enzymes are functional. Potential endoproteolytic recognition sites for proprotein convertases in the PAM sequence indicate that PAM-derived soluble isoforms may also be expressed. Sequences potentially encoding proprotein convertases (PC1 and PC2), carboxypeptidase E (CPE), and other enzymes of the α-amidation pathway, were also found, confirming the presence of this pathway in scorpions. Full article
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Open AccessArticle
A Novel Bradykinin-Related Peptide, RVA-Thr6-BK, from the Skin Secretion of the Hejiang Frog; Ordorrana hejiangensis: Effects of Mammalian Isolated Smooth Muscle
Received: 26 May 2019 / Revised: 25 June 2019 / Accepted: 25 June 2019 / Published: 28 June 2019
PDF Full-text (2218 KB) | HTML Full-text | XML Full-text
Abstract
A novel naturally-occurring bradykinin-related peptide (BRP) with an N-terminal extension, named RVA-Thr6-Bradykinin (RVA-Thr6-BK), was here isolated and identified from the cutaneous secretion of Odorrana hejiangensis (O. hejiangensis). Thereafter, in order to evaluate the difference in myotropic actions, a [...] Read more.
A novel naturally-occurring bradykinin-related peptide (BRP) with an N-terminal extension, named RVA-Thr6-Bradykinin (RVA-Thr6-BK), was here isolated and identified from the cutaneous secretion of Odorrana hejiangensis (O. hejiangensis). Thereafter, in order to evaluate the difference in myotropic actions, a leucine site-substitution variant from Amolops wuyiensis skin secretion, RVA-Leu1, Thr6-BK, was chemically synthesized. Myotropic studies indicated that single-site arginine (R) replacement by leucine (L) at position-4 from the N-terminus, altered the action of RVA-Thr6-BK from an agonist to an antagonist of BK actions on rat ileum smooth muscle. Additionally, both BK N-terminal extended derivatives (RVA-Thr6-BK and RVA-Leu1, Thr6-BK) exerted identical myotropic actions to BK, such as increasing the frequency of contraction, contracting and relaxing the rat uterus, bladder and artery preparations, respectively. Full article
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