Purification, sequencing and structural analysis of two acidic phospholipases A2 from the venom of Bothrops insularis (jararaca ilhoa)

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

“…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.…”

“…These findings are consistent with observations in most of the acidic PLA 2 s purified from snake venoms, which generally lack myotoxicity. However, some recently isolated acidic PLA 2 s display myotoxicity in vivo [14,20,21,40,47]. Although it is clear that the catalytic activity of PLA 2 s is not a sufficient requirement to generate myotoxicity per se, the structural determinants of such differences in myotoxicity among acidic enzymes are unknown, and their identification poses a challenging question.…”

A Novel Acidic Myotoxic Phospholipase A₂ of Colombian <em>B. asper</em> Venom. Isolation and Functional Characterization

“…In the same way, BinTX-I from B. insularis, also increased CK activity. Nevertheless, morphological analysis, showed BinTX-I produced less damaged proportion of fibers than the venom [10]. [15], demonstrated that BmooTX-I was able to damage plasmatic membrane formed by some types of phospholipids, mainly phosphatidylcholine, which were hydrolyzed by BmooTX-I producing free fatty acids and lysophospholipids, causing cellular damage.…”

“…Acidic PLA2s from snake venoms have not been completely studied and many of the ones that have been characterized, have been described as non-myotoxic and as inductors of other pharmacological effects, such as platelet aggregation inhibition and hypotension [10]. This paper describes the isolation and characterization of a myotoxic acidic PLA2 from B. asper venom, it was named BaCol PLA2.…”

Caracterização da reação inflamatória induzida pelo veneno da serpente Bothrops insularis: Influxo leucocitário, liberação de mediadores inflamatórios e mecanismos envolvidos nesses efeitos

“…Quanto à constituição do veneno, até o presente, foram isoladas e caracterizadas esterases (SELISTRE e GIGLIO, 1987;SELISTRE et al, 1990), um fator ativador de protrombina (insularinase A) e um componente inibidor de trombina-like tipo lectina-C (MODESTO et al, 2005;OLIVEIRA-CARVALHO et al, 2008), além de um fator de crescimento do endotélio (sv-VEGF) (JUNQUEIRA-DE-AZEVEDO et al, 2001), uma fosfolipase A 2 (fração IV) (COGO et al, 1998(COGO et al, , 2006RODRIGUES-SIMIONI et al, 2004;BRAGA et al, 2008), peptídeos potencializadores de bradicinina (CINTRA et al, 1990), bem como uma proteína do tipo lectina-C e uma L-amino oxidase (fração II) (BRAGA et al, 2006(BRAGA et al, , 2008. Ainda, a análise proteômica do veneno de B. insularis demonstra a sua composição em quatro famílias principais: metaloproteinase, serinoproteinase, fosfolipase A 2 e lectina (CIDADE et al, 2005;VALENTE et al, 2009).…”