An α-type phospholipase A2 inhibitor from Bothrops jararacussu snake plasma: Structural and functional characterization

Oliveira, Clayton Z.; Menaldo, Danilo L.; Marcussi, Silvana; Santos-Filho, Norival A.; Silveira, Lucas B.; Boldrini-França, Johara; Rodrigues, Veridiana M.; Soares, Andreimar M.

doi:10.1016/j.biochi.2008.05.009

Cited by 35 publications

(46 citation statements)

References 34 publications

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“…The CRD of αPLIs lacks the amino acid residues involved in Ca 2+ binding, making the interaction with their respective ligands Ca 2+ -independent [40, 42]. Moreover, several studies have shown that the carbohydrate motif present in αPLIs is not necessary for the connection with PLA 2 [32, 38]. …”

Section: Alpha-type Pla2 Inhibitormentioning

confidence: 99%

Alpha-type phospholipase A2 inhibitors from snake blood

Santos-Filho

Santos

2017

J Venom Anim Toxins Incl Trop Dis

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It is of popular and scientific knowledge that toxins from snake venom (among them the PLA2 and myotoxins) are neutralized by various compounds, such as antibodies and proteins purified from animal blood. Venomous and nonvenomous snakes have PLA2 inhibitory proteins, called PLIs, in their blood serum. One hypothesis that could explain the presence of these PLIs in the serum of venomous snakes would be self-protection against the enzymes of their own venom, which eventually could reach the circulatory system. However, the presence of PLIs in non-venomous snakes suggests that their physiological role might not be restricted to protection against PLA2 toxins, but could be extended to other functions, as in the innate immune system and local regulation of PLA2s. The present study aimed to review the currently available literature on PLA2 and myotoxin alpha inhibitors present in snake plasma, thus helping to improve the research on these molecules. Furthermore, this review includes current information regarding the mechanism of action of these inhibitors in an attempt to better understand their application, and proposes the use of these molecules as new models in snakebite therapy. These molecules may help in the neutralization of different types of phospholipases A2 and myotoxins, complementing the conventional serum therapy.

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Section: Alpha-type Pla2 Inhibitormentioning

confidence: 99%

Alpha-type phospholipase A2 inhibitors from snake blood

Santos-Filho

Santos

2017

J Venom Anim Toxins Incl Trop Dis

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“…)[23] Bothrops jararacussu Jararacussu (Port. )[14, 23] Bothrops moojeni Brazilian lancehead[16] Bothrops neuwiedi Jararaca pintada (Port. )[23] Cerrophidion godmani Honduras montane pit viper[21] Crotalus durissus terrificus South American rattlesnake, tropical rattlesnake[23] Gloydius brevicaudus Short-tailed mamushi, Japanese or Chinese mamushi,[19] a , [63] Lachesis muta South American bushmaster[23] Protobothrops flavoviridis Habu[25, 64, 65], [66] a Protobothrops elegans Sakishima habu[41]

a Recombinant homolog

…”

Section: Alpha Class Of Sbplis (Sbαplis)mentioning

confidence: 99%

“…Carbohydrates do not seem essential for the inhibition of PLA 2 by sbPLIs, since some of them remain functional in the absence of this moiety [16–20]. When the target PLA 2 s are Lys49 homologues or Asp49 myotoxins, the sbPLIs are specifically called myotoxin inhibitor proteins (MIPs) [13, 14, 16, 21, 22]. …”

Section: Introductionmentioning

confidence: 99%

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior

Melo

Dias

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins, although the carbohydrate moiety may not be essential for PLA2 inhibition in every case. The presently known sbPLIs belong to one of three structural classes – namely sbαPLI, sbβPLI or sbγPLI – depending on the presence of characteristic C-type lectin-like domains, leucine-rich repeats or three-finger motifs, respectively. Currently, the most numerous inhibitors described in the literature are sbαPLIs and sbγPLIs, whereas sbβPLIs are rare. When the target PLA2 is a Lys49 homolog or an Asp49 myotoxin, the sbPLI is denominated a myotoxin inhibitor protein (MIP). In this brief overview, the most relevant data on sbPLIs will be presented. Representative examples of sbαPLIs and sbγPLIs from two Old World – Gloydius brevicaudus and Malayopython reticulatus – and two New World – Bothrops alternatus and Crotalus durissus terrificus – snake species will be emphasized.

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“…Elaphe quadrivirgata e E. climacophora (OKUMURA et al, 2003;SHIRAI et al, 2009), Atropoides nummifer (QUIRÓS et al, 2007), Protobothrops flavoviridis (SHIMADA et al, 2008) e Bothrops jararacussu (OLIVEIRA et al, 2008). Os αPLIs são constituídos por mais de duas subunidades e apresentam uma região de domínio de reconhecimento de carboidrato (DRC) (DRICKAMER, 1988), que está presente em outras proteínas tais como a apoproteína surfactante pulmonar (WHITE et al, 1985), a proteína A ligante de manose de fígado de rato (DRICKAMER; DORDAL; REYNOLDS, 1986) e receptores de PLA 2 s de mamíferos (CUPILLARD et al, 1999 LIZANO et al, 1997;.…”

Section: Inibidores De Pla 2 Sunclassified

Caracterização funcional e estrutural de inibidores de fosfolipases A2 isolados do plasma de serpente Bothrops jararacussu

Oliveira¹

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An α-type phospholipase A2 inhibitor from Bothrops jararacussu snake plasma: Structural and functional characterization

Cited by 35 publications

References 34 publications

Alpha-type phospholipase A2 inhibitors from snake blood

Alpha-type phospholipase A2 inhibitors from snake blood

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Caracterização funcional e estrutural de inibidores de fosfolipases A2 isolados do plasma de serpente Bothrops jararacussu

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