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Fosfolipases A2


Estudo Funcional comparativo entre as Fosfolipases A2 ácida e básicas isoladas do veneno de Bothrops jararacussu


Marcussi, S; Urzeda, MA; Mazzi, MV; Amui, SF; Fernandes, VC; Cambraia, RS; Silveira, LB; França, SC; Soares, AM.

Depto. Análises Clínicas, Toxicológicas e Bromatológicas-FCFRP-USP, Ribeirão Preto-SP.

Atividade Fosfolipásica, atividades miotóxica, edematogênica, citotóxica sobre células endoteliais, tumorais, hipotensora, efeitos sobre a agregação plaquetária e ruptura de lipossomos.

Eventos (Congressos, Simpósios, etc)

CONIC 2003




Atividades Bactericida e Neurotóxica de duas Fosfolipases A2 Miotóxicas isoladas do veneno de Bothrops neuwiedi pauloensis


(1) Cambraia, R.S.; (2) Rodrigues, V.M.; (1) Malta-Neto., N.R.; (1,3) Marcussi, S.; (4) Sant´ana, C.D.; (1) Araújo, A.L.; (1) Silveira, L.B.; (2) Ferro, E.A.V.; (3) Giglio, J.R.; (2) Homsi-Brandebur

(1) Instituto de Genética e Bioquímica e Instituto de Ciências Biomédicas, UFU, Uberlândia-MG; (2) Unidade de Biotecnologia, UNAERP, (3) Depto Bioquímica e Imunologia, FMRP-USP e (4) Depto. Aná

Atividades Bactericida e Neurotóxica, Atividade fosfolipásica, Atividade anticoagulante, Indução de Edema

Eventos (Congressos, Simpósios, etc)

CONIC 2004




Bothrops erythromelas - ABC96692


phospholipase A2 precursor [Bothrops erythromelas].

Bothrops erythromelas

gi|86450426|gb|ABC96692.1| phospholipase A2 precursor [Bothrops erythromelas]



Bothrops jararacussu (jararacussu) - 1Z76_A


Chain A, Crystal Structure Of An Acidic Phospholipase A2 (Btha-I) From Bothrops Jararacussu Venom Complexed With P- Bromophenacyl Bromide.

Bothrops jararacussu

gi|93278528|pdb|1Z76|A Chain A, Crystal Structure Of An Acidic Phospholipase A2 (Btha-I) From Bothrops Jararacussu Venom Complexed With P- Bromophenacyl Bromide



Bothrops jararacussu (jararacussu) - 1Z76_B


Chain B, Crystal Structure Of An Acidic Phospholipase A2 (Btha-I) From Bothrops Jararacussu Venom Complexed With P- Bromophenacyl Bromide

Bothrops jararacussu

gi|93278529|pdb|1Z76|B Chain B, Crystal Structure Of An Acidic Phospholipase A2 (Btha-I) From Bothrops Jararacussu Venom Complexed With P- Bromophenacyl Bromide



Trimeresurus flavoviridis (Q92147)


Phospholipase A2 isozyme pgPLA 1b/pgPLA 2b precursor (Phosphatidylcholine 2-acylhydrolase)

Trimeresurus flavoviridis

gi|28201850|sp|Q92147|PA2P_TRIFL Phospholipase A2 isozyme pgPLA 1b/pgPLA 2b precursor (Phosphatidylcholine 2-acylhydrolase)



Naja kaouthia (PSNJ2K)


phospholipase A2 (EC 3.1.1.4) II - monocled cobra

Naja kaouthia

gi|67172|pir||PSNJ2K phospholipase A2 (EC 3.1.1.4) II - monocled cobra



Naja sagittifera (1LFJ_A)


Chain A, X-Ray Crystal Structure Of A Complex Formed Between Two Homologous Isoforms Of Phospholipase A2 From Naja Naja Sagittifera: Principle Of Molecular Association And Inactivation.

Naja sagittifera

gi|31615496|pdb|1LFJ|A Chain A, X-Ray Crystal Structure Of A Complex Formed Between Two Homologous Isoforms Of Phospholipase A2 From Naja Naja Sagittifera: Principle Of Molecular Association And Inact



In vitro antimicrobial activity of natural toxins and animal venoms tested against Burkholderia pseudomallei.


Perumal Samy RR, Gopalakrishnakone PP, Pachiappan AA, Thwin MM, Hian YE, Bow H, Chow VT, Tuck Weng JT.


ABSTRACT: BACKGROUND: Burkholderia pseudomallei are the causative agent of melioidosis. Increasing resistance of the disease to antibiotics is a severe problem in treatment regime and has led to intensification of the search for new drugs. Antimicrobial peptides are the most ubiquitous in nature as part of the innate immune system and host defense mechanism. METHODS: Here, we investigated a group of venoms (snakes, scorpions and honey bee venoms) for antimicrobial properties against two strains of Gram-negative bacteria Burkholderia pseudomallei by using disc diffusion assay for in vitro susceptibility testing. The antibacterial activities of the venoms were compared with that of the isolated L-amino acid oxidase (LAAO) and phospholipase A2 (PLA2s) enzymes. MICs were determined using broth dilution method. Bacterial growth was assessed by measurement of optical density at the lowest dilutions (MIC 0.25 mg/mL). The cell viability was measured using tetrazolium salts (XTT) based cytotoxic assay. RESULTS: The studied venoms showed high antimicrobial activity. The venoms of C. adamanteus, Daboia russelli russelli, A. halys, P. australis, B. candidus and P. guttata were equally as effective as Chloramphenicol and Cefazidime (30 ug/disc). Among those tested, phospholipase A2 enzymes (crotoxin B and daboiatoxin), showed the most potent antibacterial activity against Gram-negative (TES) bacteria. Naturally occurring venom peptides and phospholipase A2 proved to possess highly potent antimicrobial activity against Burkholderia pseudomallei. The XTT-assay results showed that the cell survival decreased with increasing concentrations (0.05-10 mg/mL) of Crotalus adamanteus venom, with no effect on the cell viability evident at 0.5 mg/mL. CONCLUSION: This antibacterial profile of snake venoms reported herein will be useful in the search for potential antibacterial agents against drug resistant microorganisms like B. pseudomallei.


BMC Infect Dis. 2006 Jun 20;6(1):100 [Epub ahead of print]

l-amino acid oxidase, snake venom, antimicrobial activity



Influence of phospholipases A2 from snake venoms on survival and neurite outgrowth in pheochromocytoma cell line PC12.


Makarova YV, Osipov AV, Tsetlin VI, Utkin YN.


To determine whether the ability to induce neurite outgrowth in rat pheochromocytoma cell line PC12 is characteristic of phospholipases of different types, we have studied the influence of phospholipase A(2) (PLA2) from cobra Naja kaouthia venom and two PLA2s from viper Vipera nikolskii venom on PC12 cells. Phospholipases from the viper venom are heterodimers in which only one of the subunits is enzymatically active, while PLA2 from the cobra venom is a monomer. It was found that all three PLA2s induce neurite outgrowth in PC12. The PLA2 from cobra venom exhibits this effect at higher concentrations as compared to the viper enzymes. We have not observed such an activity for isolated subunits of viper PLA2s, since the enzymatically active subunits have very high cytotoxicity, while the other subunits are not active at all. However, co-incubation of active and inactive subunits before addition to the cells leads to a marked decrease in cytotoxicity and to restoration of the neurite-inducing activity. It has also been shown that all enzymatically active PLA2s are cytotoxic, the PLA2 from cobra venom being the least active. Thus, for the first time we have shown that PLA2s from snake venoms can induce neurite outgrowth in PC12 cells.


Biochemistry (Mosc). 2006 Jun;71(6):678-84.

phospholipase A2, cytotoxicity, snake venom, PC12 cells, neurite outgrowth


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