Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes.

Nakashima, Kinichi; Nobuhisa, Ikuo; Deshimaru, Masanobu; Nakai, Makoto; Ogawa, Tomoya; Shimohigashi, Yasuyuki; Fukumaki, Yasuyuki; Hattori, Masahira; Sakaki, Yoshiyuki; Hattori, Satoshi

doi:10.1073/pnas.92.12.5605

Cited by 196 publications

(104 citation statements)

References 18 publications

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“…In defense of this notion, PLA 2 acts as an antimicrobial component in innate immunity, defined solely by the transcription of coding genes and limiting the ecological modification of activity from exposure history. Applicable is the work of Nakashima et al [31], whose analysis recovered rapid evolution in the nucleotide sequence of protein-coding regions of PLA 2 isozyme genes between the venom glands of two closely related viper species (Trimeresurus). Therefore, the taxonomic resemblance of PLA 2 activity is likely more evident of immunological homology than the general serum antimicrobial activity among members of Crocodylia [10].…”

Section: Discussionmentioning

confidence: 99%

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Merchant¹,

McAdon²,

Mead³

et al. 2017

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Serum samples from all 23 extant crocodilian species were tested for phospholipase A 2 (PLA 2 ) activity against nine different bacterial species. The data were used to generate a PLA 2 activity profile for each crocodilian species, and the data were used to compare the activities of the three main lineages (Alligatoridae, Crocodylidae, and Gavialidae), the seven different genera, and to compare all of the 23 individual species. The data revealed that the three lineages of crocodilians (Alligatoridae, Crocodylidae, and Gavialidae) exhibited PLA 2 activities toward nine species of bacteria that were statistically distinguishable. In addition, the PLA 2 activities of crocodilians in a specific genus tended to be more similar to other members in their genus than to members of other crocodilian genera.

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Section: Discussionmentioning

confidence: 99%

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Merchant¹,

McAdon²,

Mead³

et al. 2017

ABC

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“…The variation in the biochemical composition of snake venom occurs between closely related species or even within a species itself (Jime´nez-Porras 1964;Glenn et al 1983;Yang et al 1991;Assakura et al 1992;Daltry et al 1996;Fry et al 2002). The great diversity of snake venom toxins is due to their mode of evolution, which is subject to frequent duplication of toxin-encoding genes that is sometimes followed by functional and structural diversification (Moura-da-Silva et al 1995;Slowinski et al 1997;Afifiyan et al 1999;Chang et al 1999;Kordis and Gubensek 2000) and accelerated rates of sequence evolution (e.g., Kini and Chan 1999;Nakashima et al 1995). This diversification is possibly a result of selection for the ability to kill and digest different prey (e.g., Daltry et al 1996) or as part of a predator-prey arms race (e.g., Poran et al 1987; Heatwole and Poran 1995).…”

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Molecular Evolution and Phylogeny of Elapid Snake Venom Three-Finger Toxins

Fry

Wüster

Kini

et al. 2003

Journal of Molecular Evolution

328

288

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Abstract. Animal venom components are of considerable interest to researchers across a wide variety of disciplines, including molecular biology, biochemistry, medicine, and evolutionary genetics. The three-finger family of snake venom peptides is a particularly interesting and biochemically complex group of venom peptides, because they are encoded by a large multigene family and display a diverse array of functional activities. In addition, understanding how this complex and highly varied multigene family evolved is an interesting question to researchers investigating the biochemical diversity of these peptides and their impact on human health. Therefore, the purpose of our study was to investigate the long-term evolutionary patterns exhibited by these snake venom toxins to understand the mechanisms by which they diversified into a large, biochemically diverse, multigene family. Our results show a much greater diversity of family members than was previously known, including a number of subfamilies that did not fall within any previously identified groups with characterized activities. In addition, we found that the long-term evolutionary processes that gave rise to the diversity of three-finger toxins are consistent with the birth-and-death model of multigene family evolution. It is anticipated that this ''three-finger toxin toolkit'' will prove to be useful in providing a clearer picture of the diversity of investigational ligands or potential therapeutics available within this important family.

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“…Not all the snakebites are fatal, yet they may result in the following conditions: permanent physical disability, including limb amputation; chronic ulceration; osteomyelitis with malignant transformation; chronic renal failure; chronic pituitary-adrenal insufficiency; A 2 (PLA 2 s) and cytotoxins (CTXs) are the major components in the venom of the Russell's viper and the Indian cobra, respectively. Both are known to be encoded by multigene families that have evolved through a process of gene duplication followed by accelerated evolution in the protein coding region (7,8,19,20). Therefore, they make a family of toxins with a highly conserved structural fold but widely varying surface amino acid residues.…”

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Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka

et al. 2010

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To examine the molecular diversity of the venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka, we isolated 38 venom proteins through a combination of anion exchange chromatography followed by reversed-phase high performance liquid chromatography. From the venom of D. r. russellii we isolated 15 proteins: 5 isozymes of phospholipase A 2 (PLA 2 ), 4 serine proteases, 2 C-type lectin-like proteins, 2 l-amino acid oxidases, 1 cysteine-rich secretory protein (CRISP), and 1 metalloproteinase. From the venom of N. naja we isolated 23 proteins: 10 isoforms of cytotoxins (CTX), 7 PLA 2 isozymes, 2 muscarinic toxinlike proteins, 2 CRISPs, 1 nerve growth factor, and 1 new thrombin-like serine protease. Most of these proteins contained new amino acid sequences for each species, indicating molecular diversity in venom proteins. The entire amino acid sequences of PLA 2 3 from D. r. russellii and CTX7 from N. naja were determined. Additionally, the polymorphic amino acid residues of PLA 2 3 were preferentially localized on the potential antigenic sites. While 2 types of PLA 2 (N and S types) were found in D. r. russellii (India) and D. r. siamensis (Java), all the PLA 2 s from D. r. siamensis (Burma) were N type, and those from D. r. russellii (Sri Lanka) were primarily S type.There are approximately 600 venomous species of snakes in the world. Although there are no accurate figures for the incidence of snakebites, at least 421,000 envenomings and 20,000 deaths are estimated to occur every year according to publications on snakebite and the World Health Organization (WHO) mortality database in 2008 (14). Snakebites caused by the families of Viperidae and Elapidae are particularly dangerous to humans. Not all the snakebites are fatal, yet they may result in the following conditions: permanent physical disability, including limb amputation; chronic ulceration; osteomyelitis with malignant transformation; chronic renal failure; chronic pituitary-adrenal insufficiency; Address correspondence to: Mieko Suzuki Division of Biomolecular Chemistry, Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya, 467-8501, Japan Tel: +81-52-872-5851, Fax: +81-52-872-5857 E-mail: m.suzuki@nsc.nagoya-cu.ac.jp To avoid confusion in terms of taxonomy, the following names were used in this paper:

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Accelerated evolution in the protein-coding regions is universal in crotalinae snake venom gland phospholipase A2 isozyme genes.

Cited by 196 publications

References 18 publications

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Comparison of Serum Phospholipase A2 Activities of All Known Extant Crocodylian Species

Molecular Evolution and Phylogeny of Elapid Snake Venom Three-Finger Toxins

Molecular diversity in venom proteins of the Russell's viper (Daboia russellii russellii) and the Indian cobra (Naja naja) in Sri Lanka

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