Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Kono, Koji; Konishi, Motomi; Maruta, Yuji; Toriba, Michihisa; Sakai, Atsushi; Matsuda, Akira; Hori, Takamitsu; Nakatani, Mitsuko; Minamino, Naoto; Akizawa, Toshifumi

doi:10.2131/jts.31.157

Cited by 38 publications

(26 citation statements)

References 20 publications

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“…A novel MMP toxin had been reported previously from the venom of the lethal natricid snake Rhabdophis tigrinus (39 and was shown to be closest to MMP2 (Fig. 14) rather than showing the MMP9 relationship hypothesized in the previous R. tigrinus study.…”

Section: Isolation and Characterization Of Venom Toxin Transcripts-mentioning

confidence: 65%

Evolution of an Arsenal

Fry

Scheib²,

Weerd³

et al. 2008

Molecular & Cellular Proteomics

308

145

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Venom is a key innovation underlying the evolution of advanced snakes (Caenophidia). Despite this, very little is known about venom system structural diversification, toxin recruitment event timings, or toxin molecular evolution. A multidisciplinary approach was used to examine the diversification of the venom system and associated toxins across the full range of the ϳ100 million-year-old advanced snake clade with a particular emphasis upon families that have not secondarily evolved a front-fanged venom system (ϳ80% of the 2500 species). Analysis of cDNA libraries revealed complex venom transcriptomes containing multiple toxin types including three finger toxins, cobra venom factor, cysteine-rich secretory protein, hyaluronidase, kallikrein, kunitz, lectin, matrix metalloprotease, phospholipase A 2 , snake venom metalloprotease/a disintegrin and metalloprotease, and waprin. High levels of sequence diversity were observed, including mutations in structural and functional residues, changes in cysteine spacing, and major deletions/truncations. Morphological analysis comprising gross dissection, histology, and magnetic resonance imaging also demonstrated extensive modification of the venom system architecture in nonfront-fanged snakes in contrast to the conserved structure of the venom system within the independently evolved front-fanged elapid or viperid snakes. Further, a reduction in the size and complexity of the venom system was observed in species in which constriction has been secondarily evolved as the preferred method of prey capture or dietary preference has switched from live prey to eggs or to slugs/snails. Investigation of the timing of toxin recruitment events across the entire advanced snake radiation indicates that the evolution of advanced venom systems in three front-fanged lineages is associated with recruitment of new toxin types or explosive diversification of existing toxin types. These results support the role of venom as a key evolutionary innovation in the diversification of advanced snakes and identify a potential role for non-front-fanged venom toxins as a rich source for lead compounds for drug design and development.

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Section: Isolation and Characterization Of Venom Toxin Transcripts-mentioning

confidence: 65%

Evolution of an Arsenal

Fry

Scheib²,

Weerd³

et al. 2008

Molecular & Cellular Proteomics

308

145

View full text Add to dashboard Cite

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“…For Colubrinae, transcriptomes of oral glands from Pantherophis guttatus, Opheodrys aestivus [9] and Boiga irregularis (Duvernoy’s venom gland); [12] were generated, although only the last one was complemented by venom proteomic analysis. Nevertheless, many toxins from the other subfamilies have been investigated by more focused approaches, such as protein purification from the venom (e.g., Borikenophis portoricensis [47]) or specific cDNA cloning, including some genera with particularly toxic venom, such as the natricine Rhabdophis [66]. Very recently, full length mRNAs derived from secreted venoms of several colubrine and dipsadine colubrids were reverse transcribed and sequenced, demonstrating that it is possible to obtain transcript sequences from venom alone [67].…”

Section: Resultsmentioning

confidence: 99%

Colubrid Venom Composition: An -Omics Perspective

Junqueira-de-Azevedo

Campos

Ching

et al. 2016

Toxins

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Snake venoms have been subjected to increasingly sensitive analyses for well over 100 years, but most research has been restricted to front-fanged snakes, which actually represent a relatively small proportion of extant species of advanced snakes. Because rear-fanged snakes are a diverse and distinct radiation of the advanced snakes, understanding venom composition among “colubrids” is critical to understanding the evolution of venom among snakes. Here we review the state of knowledge concerning rear-fanged snake venom composition, emphasizing those toxins for which protein or transcript sequences are available. We have also added new transcriptome-based data on venoms of three species of rear-fanged snakes. Based on this compilation, it is apparent that several components, including cysteine-rich secretory proteins (CRiSPs), C-type lectins (CTLs), CTLs-like proteins and snake venom metalloproteinases (SVMPs), are broadly distributed among “colubrid” venoms, while others, notably three-finger toxins (3FTxs), appear nearly restricted to the Colubridae (sensu stricto). Some putative new toxins, such as snake venom matrix metalloproteinases, are in fact present in several colubrid venoms, while others are only transcribed, at lower levels. This work provides insights into the evolution of these toxin classes, but because only a small number of species have been explored, generalizations are still rather limited. It is likely that new venom protein families await discovery, particularly among those species with highly specialized diets.

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“…Column Switch (CS)-HPLC System The CS-HPLC method used here was modified from the method reported previously, 46) and consisted of an affinity column (TSKgel Chelate-5PW, 75 mmϫ7.5 mm i.d. ; Tosoh, Japan) for the first separation and an octadecylsilica (ODS) reversed-phase column (Cosmosil 5C 18 -MS-II, 150 mmϫ4.6 mm i.d.…”

Section: Methodsmentioning

confidence: 99%

Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

Kojima

Konishi

et al. 2011

CHEMICAL & PHARMACEUTICAL BULLETIN

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Regular ArticlePrion protein (PrP) is a cell-surface glycoprotein implicated in the pathogenesis of a range of neurodegenerative disorders collectively termed transmissible spongiform encephalopathies (TSEs), including Creutzfeldt-Jakob disease (CJD) in humans, bovine spongiform encephalopathy (BSE) in cows, and chronic wasting disease (CWD) in deer.1-4) PrP exists in two distinct forms: cellular PrP (PrP C ) and a pathogenic or scrapie form (PrP Sc ) derived from PrP C . Although there is no difference in the primary structure of these isoforms, spectroscopic studies revealed that PrP C has a high ahelical content, whereas PrP Sc is composed primarily of bsheets. 5,6) There are many hypotheses regarding the conversion of PrP C to PrP Sc , but the data suggest that conversion is entirely conformational and involves no amino acid substitutions or deletions, and thus supports the protein-only hypothesis.2) Prion replication requires the conversion of PrP C into PrP Sc , where PrP Sc acts as a template and protein X functions as a chaperone. [7][8][9] Mature human PrP (hPrP) consists of 253 amino acids, with a C-terminal glycosylphosphatidylinositol (GPI) anchor and two glycosylation sites (Fig. 1). The N-terminal domain, which includes four repeats of the PHGGGWGQ octapeptide, is a flexibly disordered region. In contrast, the C-terminal domain, which includes two a-helices and a GPI anchor, is a folded region. The middle domain includes two b-sheets and one a-helix.10-12) The hPrP region spanning amino acid residues 106-126 in the middle domain is thought to be responsible for the pathogenic properties of PrP Sc , including neurotoxicity, protease-resistance, induction of hypertrophy, and promotion of astrocyte proliferation. [13][14][15][16][17] Although PrP metal-binding sites have been investigated using full-length PrP C or synthetic fragment peptides and it is now generally accepted that PrP C binds copper in vivo, 18) most researchers have focused on the octarepeat region, [19][20][21][22][23] and there are few reports describing the metal-binding ability of the middle-and C-terminal domains of hPrP.24) The interaction of full-length and truncated forms of PrP with Cu 2+ has been investigated using a range of techniques, including electron paramagnetic resonance (EPR), [25][26][27] We developed a column switch (CS)-HPLC system that can detect direct metal-binding to the octarepeat region of hPrP C , and the data obtained using our CS-HPLC method agreed well with previous CD analyses. 42,43) In this study, we used CS-HPLC to analyze the metal-binding characteristics of 21 synthetic fragment peptides derived from the sequence of hPrP amino acids 60-230. Key words prion protein; metal-binding; metal chelate affinity column; column switch HPLC; synthetic peptide Chem. Pharm. Bull. 59(8) 965-971 (2011)

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Characterization of a Novel Metalloproteinase in Duvernoy's Gland of Rhabdophis Tigrinus Tigrinus

Cited by 38 publications

References 20 publications

Evolution of an Arsenal

Evolution of an Arsenal

Colubrid Venom Composition: An -Omics Perspective

Metal-Binding Ability of Human Prion Protein Fragment Peptides Analyzed by Column Switch HPLC

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