Geographic variations, cloning, and functional analyses of the venom acidic phospholipases A2 of Crotalus viridis viridis

Tsai, Inn-Ho; Wang, Ying Ming; Chen, Yi Hsuan; Tu, Anthony T.

doi:10.1016/s0003-9861(02)00747-6

Cited by 45 publications

(52 citation statements)

References 31 publications

(42 reference statements)

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“…Cdc-PLA 2 possesses high similarity with a subgroup of acidic D49-PLA 2 s which is expressed in the venom as monomers and/or as homodimers (42)(43)(44)(45). In fact, the ability of an acidic glycosylated and phosphorylated PLA 2 s to co-exist in snake venom as monomer and homodimer was recently described by Sun et al (27).…”

Section: Discussionmentioning

confidence: 94%

“…Acidic IIA phospholipases A 2 present multiple isoforms, generally associated with intra-specific geographic variation, as well as adaptation to prey diversity (43,44,54,55). On the other hand, some PLA 2 clones apparently not translated into venom proteins has been reported, since not-expressing toxin mRNA may be a repository for snake survival under an ever-changing environment (54,55).…”

Section: Discussionmentioning

confidence: 99%

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Cloning of a novel acidic phospholipase A2 from the venom gland of Crotalus durissus cascavella (Brazilian northeastern rattlesnake)

Guarnieri¹,

Melo²,

Melo³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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The phospholipase A2 superfamily encompasses 15 groups that are classified into: secreted PLA2 (sPLA2); cytosolic PLA2 (cPLA2); Ca2+-independent intracellular PLA2 (iPLA2); platelet-activating factor acetylhydrolase (PAF-AH); and lysosomal PLA2. Currently, approximately 700 PLA2 sequences are known, of which 200 are obtained from the venom gland of Crotalinae snakes. However, thus far, little information is available on cloning, purification and structural characterization of PLA2 from Crotalus durisssus cascavela venom gland. In the present work, we report the molecular cloning of a novel svPLA2 from C. d. cascavella (Cdc), a predominant rattlesnake subspecies in northeastern Brazil. The Cdc svPLA2 cDNA precursor is 689 nucleotides long and encodes a protein of 138 amino acid residues, with a calculated molecular mass of approximately 13,847 Da and an estimated isoelectric point of 5.14. Phylogenetic analysis of Crotalinae PLA2 reveals that Cdc PLA2 clustered with other acidic type IIA PLA2 homologues is also present in the venom of North American rattlesnakes. Hitherto, this study presents a novel PLA2 cDNA precursor from C. d. cascavella and data reported herein will be useful for further steps in svPLA2 purification and analysis

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

Cloning of a novel acidic phospholipase A2 from the venom gland of Crotalus durissus cascavella (Brazilian northeastern rattlesnake)

Guarnieri¹,

Melo²,

Melo³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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“…In addition, ontogenetic and geographical variations have been noticed in the venom proteomes of other snakes, i.e. Crotalus viridis viridis [42], C.v. oreganus [43,44], Bothrox atrox [45,46], and Bothrops asper [46], and might represent a common phenomenon in many other species (see below). Alternatively, the nonvenom-secreted or very low abundance (b0.05% of the total venom proteins), toxins may play a hitherto unrecognized physiological function in the venom gland, or may simply represent a hidden repertoire of orphan molecules which may eventually become functional for the adaptation of snakes to changing ecological niches and prey habits.…”

Section: Proteomic Vs Transcriptomic Of L Muta Venommentioning

confidence: 99%

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Sanz

Escolano

Ferretti

et al. 2008

Journal of Proteomics

124

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This article appeared in a journal published by Elsevier. The attached copy is furnished to the author for internal non-commercial research and education use, including for instruction at the authors institution and sharing with colleagues.Other uses, including reproduction and distribution, or selling or licensing copies, or posting to personal, institutional or third party websites are prohibited. were identified in L. muta and L. stenophrys venoms. In addition, both venoms contained a large number of bradykinin-potentiating peptides (BPP) and a C-type natriuretic peptide (C-NP). BPPs and C-NP comprised around 15% of the total venom proteins. In both species, the most abundant proteins were Zn 2+ -metalloproteinases (32-38%) and serine proteinases (25-31%), followed by PLA 2 s (9-12%), galactose-specific C-type lectin (4-8%), L-amino acid oxidase (LAO, 3-5%), CRISP (1.8%; found in L. muta but not in L. stenophrys), and NGF (0.6%).On the other hand, only six L. muta venom-secreted proteins matched any of the previously reported 11 partial or full-length venom gland transcripts, and venom proteome and transcriptome depart in their relative abundances of different toxin families. As expected from their close phylogenetic relationship, the venoms of L. muta and L. stenophrys share (or contain highly similar) proteins, in particular BPPs, serine proteinases, a galactose-specific C-type lectin, and LAO. However, they dramatically depart in their respective PLA 2 complement. Intraspecific quantitative and qualitative differences in the expression of PLA 2 molecules were found when the venoms of five L. muta specimens (3 from Bolivia and 2 from Peru) and the venom of the same species purchased from Sigma were compared.These observations indicate that these class of toxins represents a rapidly-evolving Author's personal copy gene family, and suggests that functional differences due to structural changes in PLA 2 s molecules among these snakes may have been a hallmark during speciation and adaptation of diverging snake populations to new ecological niches, or competition for resources in existing ones. Our data may contribute to a deeper understanding of the biology and ecology of these snakes, and may also serve as a starting point for studying structure-function correlations of individual toxins.

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“…The known members of this venom PLA 2 subtype include the basic subunits of crotoxin and mojave toxin, agkistrodotoxin from Gloydius halys brevicaudus (formerly Agkistrodon halys Pallas) [11], trimucrotoxin from Protobothrops mucrosquamatus [12], Tf-PLA-N from P. flavoviridis [13] and the myotoxin from Crotalus viridis viridis (designated as Cvv-N6) [14,15]. In the present study, we purified and sequenced six novel N6-PLA 2 s from the New World pit viper venoms, and identified several N6-PLA 2 neurotoxins from the Asian pit viper venoms.…”

Section: Introductionmentioning

confidence: 99%

Molecular evolution and structure–function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms

Chen

Wang

Hseu

et al. 2004

Biochemical Journal

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Some myotoxic or neurotoxic PLA 2 s (phospholipases A 2 ) from pit viper venoms contain characteristic N6 substitutions. Our survey of the venoms of more than ten pit viper genera revealed that N6-PLA 2 s exist only in limited Asian pit vipers of two genera, Protobothrops and Gloydius, and exist as either monomers or the basic subunits of heterodimers in some New World pit vipers. For the newly identified N6-PLA 2 s, the neuromuscular blocking activities were assayed with the chick biventer cervicis neuromuscular tissue, whereas the increased serum creatine kinase level assessed their myotoxicities. The purified N6-PLA 2 s from Protobothrops mangshanensis and Gloydius intermedius saxatilis were found to be presynaptic neurotoxins. In contrast, all N6-PLA 2 s from the venoms of Sistrurus miliarius strackeri, S. m. barbouri, Crotalus viridis viridis, C. lepidus lepidus, Cerrophidion godmani and Bothreichis schlegelii were myotoxins without neurotoxicity even in the presence of crotoxin A. Crotoxin-like complexes were for the first time purified from the venoms of Sitrurus catenatus tergeminus, C. mitchelli mitchelli, C. horridus atricaudatus, C. basiliscus and C. durissus cumanensis. The cDNAs encoding six novel N6-PLA 2 s and subunits of the crotoxin-like complex from S. c. tergeminus were cloned and fully sequenced. Phylogeny analysis showed that two structural subtypes of N6-PLA 2 s with either F24 or S24 substitution have been evolved in parallel, possibly descended respectively from species related to present-day Protobothrops and Gloydius. Calmodulin binds all the N6-PLA 2 s but crotoxin A may inhibit its binding to crotoxin B and to other neurotoxic N6-PLA 2 s. Structure-activity relationships at various regions of the PLA 2 molecules were extensively discussed.

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Geographic variations, cloning, and functional analyses of the venom acidic phospholipases A2 of Crotalus viridis viridis

Cited by 45 publications

References 31 publications

Cloning of a novel acidic phospholipase A2 from the venom gland of Crotalus durissus cascavella (Brazilian northeastern rattlesnake)

Cloning of a novel acidic phospholipase A2 from the venom gland of Crotalus durissus cascavella (Brazilian northeastern rattlesnake)

Snake venomics of the South and Central American Bushmasters. Comparison of the toxin composition of Lachesis muta gathered from proteomic versus transcriptomic analysis

Molecular evolution and structure–function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pit viper venoms

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