A Novel Phospholipase A2, BJ-PLA2, from the Venom of the Snake Bothrops jararaca: Purification, Primary Structure Analysis, and Its Characterization as a Platelet-Aggregation-Inhibiting Factor

Serrano, Solange M.T.; Reichl, Antonia P.; Mentele, Reinhard; Auerswald, Ennes A.; Santoro, Marcelo Larami; Sampaio, Cláudio Hoffmann; Camargo, Antônio Carlos Martins de; Assakura, Marina T.

doi:10.1006/abbi.1999.1230

Cited by 60 publications

(41 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The primary structure of BaspPLA 2 -II presents high identity values in comparison to other acidic enzymes within the genus Bothrops, particularly P81243 from B. jararaca [19], Q8QG87 from B. insularis [40], and Q8AXY1 from B. jararacussu [17]. Of these, only the PLA 2 from B. jararaca shares with BaspPLA 2 -II the feature of having 124 amino acids (as opposed to the pattern of 122 residues of most of these enzymes), caused by two insertions at positions 67 and 68.…”

Section: Discussionmentioning

confidence: 99%

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

et al. 2010

View full text Add to dashboard Cite

a b s t r a c tPhospholipases A 2 (PLA 2 ) are major components of snake venoms, exerting a variety of relevant toxic actions such as neurotoxicity and myotoxicity, among others. Since the majority of toxic PLA 2 s are basic proteins, acidic isoforms and their possible roles in venoms are less understood. In this study, an acidic enzyme (BaspPLA 2 -II) was isolated from the venom of Bothrops asper (Pacific region of Costa Rica) and characterized. BaspPLA 2 -II is monomeric, with a mass of 14,212 AE 6 Da and a pI of 4.9. Its complete sequence of 124 amino acids was deduced through cDNA and protein sequencing, showing that it belongs to the Asp49 group of catalytically active enzymes. In vivo and in vitro assays demonstrated that BaspPLA 2 -II, in contrast to the basic Asp49 counterparts present in the same venom, lacks myotoxic, cytotoxic, and anticoagulant activities. BaspPLA 2 -II also differed from other acidic PLA 2 s described in Bothrops spp. venoms, as it did not show hypotensive and anti-platelet aggregation activities. Furthermore, this enzyme was not lethal to mice at intravenous doses up to 100 mg (5.9 mg/g), indicating its lack of neurotoxic activity. The only toxic effect recorded in vivo was a moderate induction of local edema. Therefore, the toxicological characteristics of BaspPLA 2 -II suggest that it does not play a key role in the pathophysiology of envenomings by B. asper, and that its purpose might be restricted to digestive functions. Immunochemical analyses using antibodies raised against BaspPLA 2 -II revealed that acidic and basic PLA 2 s form two different antigenic groups in B. asper venom.

show abstract

Section: Discussionmentioning

confidence: 99%

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

et al. 2010

View full text Add to dashboard Cite

show abstract

“…Although studies involving snake venom acidic PLA 2 s have increased considerably in the recent years, only a few acidic PLA 2 s from Brazilian snake venoms were purified and cloned (18,21,(35)(36)(37)(38)(39)(40)(41). Up to date, nothing was known about the expression of acidic (subgroup II) PLA 2 in the venom gland of Crotalus durissus cascavella.…”

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

View full text Add to dashboard Cite

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

show abstract

“…As PLA 2 s catalisam a hidrólise de 2-sn-fosfolipídeos em ácidos graxos e lisofosfolipídeos, a qual está relacionada com importantes atividades farmacológicas, tais como efeito sobre plaquetas, neurotoxicidade, atividade anticoagulante e miotoxicidade (OHNO et al, 2003;GUTIÉRREZ e OWNBY, 2003;SANTOS-FILHO et al, 2008;DE PAULA et al, 2009 (GUTIÉRREZ e LOMONTE, 1995;OWNBY et al, 1999;SOARES et al, 2004a,b;PONCE-SOTO et al, 2006;ABREU et al, 2007). Por outro lado, as PLA 2 s ácidas presentes nas peçonhas de serpentes deste gênero foram pouco estudadas e pouco se sabe sobre o mecanismo de ação destas enzimas (SERRANO et al, 1999;ANDRIÃO-ESCARSO et al, 2002;FULY et al, 2002;COGO et al, 2006;DE ALBUQUERQUE MODESTO et al, 2006;RODRIGUES et al, 2007;TEIXEIRA et al, 2011).…”

Section: Fosfolipases a 2 De Peçonhas De Serpentesunclassified

“…Em geral, as PLA 2 s ácidas de Bothrops não apresentam efeitos tóxicos diretos sobre tecidos, mas induzem importantes efeitos farmacológicos como inibição da agregação plaquetária e hipotensão arterial (SERRANO et al, 1999;ANDRIÃO-ESCARSO et al, 2002;ROBERTO et al, 2004a, b;TEIXEIRA et al, 2009;GARCIA-DENEGRI et al, 2010). Entretanto, algumas exceções foram descritas como: uma PLA 2 de Bothrops alternatus que induz hemorragia pulmonar e necrose em células do músculo cardíaco de murinos (NISENBOM et al, 1986; e outra recentemente isolada de Bothrops pauloensis, denominada Bp-PLA 2 que induz mionecrose .…”

Section: Fosfolipases a 2 De Peçonhas De Serpentesunclassified

“…Esta composição pode explicar a capacidade desta região de interagir e penetrar nas camadas lipídicas das membranas celulares, uma propriedade relacionada com a atividade miotóxica dessas toxinas. Já nas PLA 2 s Asp49, a região C-terminal é composta predominantemente por resíduos hidrofílicos e aniônicos VALENTIN e LAMBEAU 2000;LOMONTE et al, 2003;OHNO et al, 2003;DOS SANTOS et al, 2009;TEIXEIRA et al ,2011 (FULY et al, 1997;SERRANO et al, 1999;ANDRIÃO-ESCARSO et al, 2002;KETELHUT et al, 2003;ROBERTO et al, 2004a, b ;MAGRO et al, 2003;COGO et al, 2006;MODESTO et al, 2006;RODRIGUES et al, 2007TEIXEIRA et al, 2011). A aquisição de informações adicionais irá contribuir para a melhor compreensão dos mecanismos de ação destas enzimas individualmente e da sua participação em envenenamentos ofídicos.…”

Section: Caracterização Estruturalunclassified

See 1 more Smart Citation

Caracterização funcional e estrutural de uma nova fosfolipase A2 ácida de Bothrops moojeni

Silveira¹

View full text Add to dashboard Cite

A Novel Phospholipase A2, BJ-PLA2, from the Venom of the Snake Bothrops jararaca: Purification, Primary Structure Analysis, and Its Characterization as a Platelet-Aggregation-Inhibiting Factor

Cited by 60 publications

References 39 publications

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

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

Caracterização funcional e estrutural de uma nova fosfolipase A2 ácida de Bothrops moojeni

Contact Info

Product

Resources

About