A protective immune response against lethal, dermonecrotic and hemorrhagic effects of Loxosceles intermedia venom elicited by a 27-residue peptide

Dias-Lopes, Camila; Guimarães, Gabriela; Felicori, Liza; Fernandes, P; Emery, Luiz Eduardo C.; Kalapothakis, Evanguedes; Nguyen, Christophe; Molina, Franck; Granier, Claude; Chávez-Olórtegui, Carlos

doi:10.1016/j.toxicon.2009.09.019

Cited by 34 publications

(19 citation statements)

References 31 publications

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“…The cross-reactivity of humoral response might be an interesting point for studies in therapeutic antivenom or vaccine development (Felicori et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

“…To cope with this, the use of synthetic non-toxic peptides can be an alternative approach to generate serum or vaccines against toxins. In fact, the use of synthetic peptides, corresponding to defined parts of the amino acid sequence (epitopes) of certain toxins can actually lead to anti-venom preparation (Alvarenga et al, 2002;Felicori et al, 2009). …”

Section: Introductionmentioning

confidence: 99%

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Identification and characterization of B-cell epitopes of 3FTx and PLA2 toxins from Micrurus corallinus snake venom

Castro

Duarte

Ramos

et al. 2015

Toxicon

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The main goal of this work was to develop a strategy to identify B-cell epitopes on four different three finger toxins (3FTX) and one phospholipase A2 (PLA2) from Micrurus corallinus snake venom. 3FTx and PLA2 are highly abundant components in Elapidic venoms and are the major responsibles for the toxicity observed in envenomation by coral snakes. Overlapping peptides from the sequence of each toxin were prepared by SPOT method and three different anti-elapidic sera were used to map the epitopes. After immunogenicity analysis of the spot-reactive peptides by EPITOPIA, a computational method, nine sequences from the five toxins were chemically synthesized and antigenically and immunogenically characterized. All the peptides were used together as immunogens in rabbits, delivered with Freund's adjuvant for a first cycle of immunization and Montanide in the second. A good antibody response against individual synthetic peptides and M. corallinus venom was achieved. Anti-peptide IgGs were also cross-reactive against Micrurus frontalis and Micrurus lemniscatus crude venoms. In addition, anti-peptide IgGs inhibits the lethal and phospholipasic activities of M. corallinus crude venom. Our results provide a rational basis to the identification of neutralizing epitopes on coral snake toxins and show that their corresponding synthetic peptides could improve the generation of immuno-therapeutics. The use of synthetic peptide for immunization is a reasonable approach, since it enables poly-specificity, low risk of toxic effects and large scale production.

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“…The cross-reactivity of humoral response might be an interesting point for studies in therapeutic antivenom or vaccine development (Felicori et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and characterization of B-cell epitopes of 3FTx and PLA2 toxins from Micrurus corallinus snake venom

Castro

Duarte

Ramos

et al. 2015

Toxicon

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“…Moreover, therapeutic serum development and vaccination have been studied to ascertain the benefits of antivenom [85,86]. Synthetic peptides designed based on PLDs toxins with specific biological/protective effects have also been utilized [87,88]. Additionally, brown spider PLDs could be employed in the development of a vaccine derived from the phospholipase-D-mutated toxin from L. intermedia (substitution of the Histidine12 for Alanine in the catalytic site—LiRecDT1H12A) for the immunization of people living in regions that are endemic for accidents involving Loxosceles spiders.…”

Section: Phospholipase-dmentioning

confidence: 99%

Brown Spider (Loxosceles genus) Venom Toxins: Tools for Biological Purposes

Chaim

Trevisan-Silva

Chaves-Moreira

et al. 2011

Toxins

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Venomous animals use their venoms as tools for defense or predation. These venoms are complex mixtures, mainly enriched of proteic toxins or peptides with several, and different, biological activities. In general, spider venom is rich in biologically active molecules that are useful in experimental protocols for pharmacology, biochemistry, cell biology and immunology, as well as putative tools for biotechnology and industries. Spider venoms have recently garnered much attention from several research groups worldwide. Brown spider (Loxosceles genus) venom is enriched in low molecular mass proteins (5–40 kDa). Although their venom is produced in minute volumes (a few microliters), and contain only tens of micrograms of protein, the use of techniques based on molecular biology and proteomic analysis has afforded rational projects in the area and permitted the discovery and identification of a great number of novel toxins. The brown spider phospholipase-D family is undoubtedly the most investigated and characterized, although other important toxins, such as low molecular mass insecticidal peptides, metalloproteases and hyaluronidases have also been identified and featured in literature. The molecular pathways of the action of these toxins have been reported and brought new insights in the field of biotechnology. Herein, we shall see how recent reports describing discoveries in the area of brown spider venom have expanded biotechnological uses of molecules identified in these venoms, with special emphasis on the construction of a cDNA library for venom glands, transcriptome analysis, proteomic projects, recombinant expression of different proteic toxins, and finally structural descriptions based on crystallography of toxins.

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“…Anti-SMasesD antibodies have been detected in sera samples from human patients after spider bite [6], confirming that these proteins might have great potential for the development of vaccines, therapeutics and diagnostics in Loxoscelism. Besides, SMaseD antigens, administered as recombinant proteins (recLiD1) or their corresponding synthetic peptides, are protective against Loxosceles experimental envenomations in rabbits [8,25], mice [10] and horses [26]. These studies suggest variability of continuous B-cell epitopes of this toxin can depend to the animals used to raise antibodies [8,10].…”

Section: Discussionmentioning

confidence: 99%

“…In addition, the region 37 FDDNANPEYTYHGIP 51 extended in its N-terminal in 12 residues has already been identified as BC epitope and mice and rabbit immunizations with it were able to protect these animals against the lethal and toxic effects of Loxosceles venom [10,25] AAYKKKFRVATYDDN 273 encompass the SMD-tail of LiD1, a Cterminal region conserved among all SMasesD described [19].…”

Section: Discussionmentioning

confidence: 99%

Protective antibodies against a sphingomyelinase D from Loxosceles intermedia spider venom elicited in mice with different genetic background

Oliveira¹,

Vilela²,

Coura³

et al. 2016

Vaccine

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A protective immune response against lethal, dermonecrotic and hemorrhagic effects of Loxosceles intermedia venom elicited by a 27-residue peptide

Cited by 34 publications

References 31 publications

Identification and characterization of B-cell epitopes of 3FTx and PLA2 toxins from Micrurus corallinus snake venom

Identification and characterization of B-cell epitopes of 3FTx and PLA2 toxins from Micrurus corallinus snake venom

Brown Spider (Loxosceles genus) Venom Toxins: Tools for Biological Purposes

Protective antibodies against a sphingomyelinase D from Loxosceles intermedia spider venom elicited in mice with different genetic background

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