Accelerated evolution of crotalinae snake venom gland serine proteases

Deshimaru, Masanobu; Ogawa, Tomoya; Nakashima, Kin Ichi; Nobuhisa, Ikuo; Chijiwa, Takahito; Shimohigashi, Yasuyuki; Fukumaki, Yasuyuki; Niwa, Mineo; Yamashina, Ikuo; Hattori, Satoshi; Ohno, Motonori

doi:10.1016/s0014-5793(96)01144-1

Cited by 165 publications

(109 citation statements)

References 29 publications

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“…Although our library is PCR-amplified, it is clear that the base changes observed in different contigs, including contig 34 or 60 and others are not artefactual. In fact, similar base changes have been found for all individual sequences of a given contig; actually, this diversity can be explained by accelerated evolution that has been well-documented in snake venom glands (Deshimaru et al, 1996). It is also known that PCR based libraries which cDNAs have not been size-fractioned may be enriched with small cDNAs.…”

Section: A Catalog Toward the Full-length Cdna And Proteins From The mentioning

confidence: 67%

Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins

Francischetti

My-Pham

Harrison

et al. 2004

Gene

107

102

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The venom gland of the snake Bitis gabonica (Gaboon viper) was used for the first time to construct a unidirectional cDNA phage library followed by high-throughput sequencing and bioinformatic analysis. Hundreds of cDNAs were obtained and clustered into contigs. We found mostly novel full-length cDNA coding for metalloproteases (P-II and P-III classes), Lys49-phospholipase A2, serine proteases with essential mutations in the active site, Kunitz protease inhibitors, several C-type lectins, bradykinin-potentiating peptide, vascular endothelial growth factor, nucleotidases and nucleases, nerve growth factor, and L-amino acid oxidases. Two new members of the recently described short coding region family of disintegrin, displaying RGD and MLD motifs are reported. In addition, we have identified for the first time a cytokine-like molecule and a multi-Kunitz protease inhibitor in snake venoms. The CLUSTAL alignment and the unrooted cladograms for selected families of B. gabonica venom proteins are also presented. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be identified. This paper also reports the N-terminus of the 15 most abundant venom proteins and the sequences matching their corresponding transcripts. The electronic version of this manuscript, available on request, contains spreadsheets with hyperlinks to FASTAformatted files for each contig and the best match to the GenBank and Conserved Domain Databases, in addition to CLUSTAL alignments of each contig. We have thus generated a comprehensive catalog of the B. gabonica venom gland, containing for each secreted protein: i) the predicted molecular weight, ii) the predicted isoelectric point, iii) the accession number, and iv) the putative function. The role of these molecules is discussed in the context of the envenomation caused by the Gaboon viper.

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Section: A Catalog Toward the Full-length Cdna And Proteins From The mentioning

confidence: 67%

Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins

Francischetti

My-Pham

Harrison

et al. 2004

Gene

107

102

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“…Thus, CLPs with diverse activities appear to be derived from a common ancestor. In this connection, IX/X-bp and IX-bp from habu snake venom have diversified their amino acid sequences in an accelerating manner (11) as also observed for crotalinae snake venom gland phospholipases (12) and serine proteases (13). As shown for the digestive enzymes in venom, which vary predictably in response to differences in diet (14), CLPs have evolved possibly to gain functional diversity in response to important components in the hemostatic system of their prey.…”

mentioning

confidence: 80%

Crystal Structure of von Willebrand Factor A1 Domain Complexed with Snake Venom, Bitiscetin

Maita

Nishio

Nishimoto

et al. 2003

Journal of Biological Chemistry

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“…Sequence comparison of the peptide containing Nterminal region of TLBbar with several other venom thrombin-like enzymes shows high degree of homology (Figure 3), in particular with Calobin thrombin-like isolated from Agkistrodon caliginosus [34], Crotalase from Crotalus adamanteus [35], and Flavoxobin from Trimeresurus flavoviridis [36]. The other two tryptic peptides have Cys170 and His57 residues highly conserved in the sequence of serine proteases [16].…”

Section: Discussionmentioning

confidence: 99%

Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity fromBothrops barnettiSnake Venom

et al. 2013

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A thrombin-like enzyme named TLBbar was isolated from Bothrops barnetti snake venom and its biochemical and pharmacological characteristics were determined. TLBbar was purified using size exclusion chromatography and reverse phase HPLC, showing molecular mass of 28750.7 Da determined by mass spectrometry. TLBbar serine protease is basic (pI 7.4) and its structure shows similarity with other serine proteases of snake venom. Optimal proteolytic activity was at 37 ∘ C and pH 8; this activity was strongly inhibited by PMSF and Leupeptin, however; heparin, and soybean trypsin inhibitor (SBT-I) were ineffective. Kinetic studies on BApNA chromogenic substrate have revealed that TLBbar presents a Michaelis-Menten kinetics, with values of and max of 0.433 mM and 0.42 nmol/min, respectively. TLBbar showed high clotting activity upon bovine and human plasma, presenting IC of 125 and minimum dose coagulant (MDC) of 2.23 g/ L. TLBbar cleavages the A chain of bovine fibrinogen, with maximal efficiency at 30-40 ∘ C in the presence of calcium after two hours incubation; this fibronogenolityc activity was inhibited by PMSF and Leupeptin, confirming its classification in the group of serine proteases. In addition, TLBbar is capable of aggregating platelets in the same way that thrombin in concentrations of 2.5 g/ L.

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Accelerated evolution of crotalinae snake venom gland serine proteases

Cited by 165 publications

References 29 publications

Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins

Bitis gabonica (Gaboon viper) snake venom gland: toward a catalog for the full-length transcripts (cDNA) and proteins

Crystal Structure of von Willebrand Factor A1 Domain Complexed with Snake Venom, Bitiscetin

Biochemical and Pharmacological Characterization of TLBbar, a New Serine Protease with Coagulant Activity fromBothrops barnettiSnake Venom

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