Isolation and complete amino acid sequence of two fibrinolytic proteinases from the toxic Saturnid caterpillar Lonomia achelous

Amarant, Tany; Burkhart, William; LeVine, Harry; Arocha-Piñango, Carmen Luisa; Parikh, Indu

doi:10.1016/0167-4838(91)90128-m

Cited by 56 publications

(23 citation statements)

References 15 publications

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“…The precipitate containing F(abЈ) 2 , native immunoglobulins, and irrelevant proteins was dissolved in 0.15 M NaCl and dialyzed against 0.15 M NaCl until complete removal of ammonium sulfate. The preparations were analyzed for the presence of F(abЈ) 2 and specific antibodies against Lonomia antigens, and submitted to quality control procedure to verify absence of bacterial contamination, bacterial endotoxin and toxic substances. The final product was adjusted to contain the desired neutralizing antibody titer in less than 10 mg of protein/ml, and labeled as antilonomic serum.…”

Section: Animalsmentioning

confidence: 99%

“…Marked alterations of blood clotting, including decreased fibrinogen, factor V, factor XIII, plasminogen, and ␣ 2 anti-plasmin, and increases in fibrinolytic activity, fibrinogen degradation products and activated thrombin may occur. [1][2][3][4][5][6] Attempts at reversing these clinical manifestations with anti-fibrinolytic drugs such as aprotinin and ⑀-aminocaproic acid associated with whole blood, freshfrozen plasma or cryoprecipitates, failed and indeed instead of reversing exacerbated them. 1,7 We and others have shown that L. obliqua caterpillar bristle extracts retain biological properties such as procoagulant activity, [2][3][4]8,9 complement (C) activation and phospholipase A 2 activity (Rocha-Campos AC and others, unpublished data).…”

Section: Introductionmentioning

confidence: 99%

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Specific heterologous F(ab')2 antibodies revert blood incoagulability resulting from envenoming by Lonomia obliqua caterpillars.

Rocha-Campos¹,

Gonçalves²,

Higashi³

et al. 2001

The American Journal of Tropical Medicine and Hygiene

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Abstract. Contact with Lonomia obliqua caterpillars results in a bleeding syndrome characterized by hemorrhage and blood coagulation disturbances. Conventional therapy using antifibrinolytics or cryoprecipitates has been unable to treat pathophysiologic alterations. As antivenoms are effective therapy for treatment of victims of venomous animals, a process of manufacturing a specific antilonomic serum by immunizing horses with Lonomia caterpillar bristle extracts (LBE) was developed. Lonomia caterpillar bristle extracts exhibited several protein bands on SDS-PAGE, induced blood coagulation abnormalities and lethality in mice, and stimulated specific antibody production in horses. Sera obtained from immunized horses were rich in anti-LBE specific antibodies distributed among the horse IgG isotypes. These antibodies had the ability to recognize various LBE antigens as well as to neutralize their coagulopathy-inducing activity. The antivenom manufactured by the developed process was composed of purified and sterilized F(abЈ) 2 with ED 50 ϭ 38.61 l, potency ϭ 0.29 mg / ml, and 95% confidence limit of potency 0.20-1.36.

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Section: Animalsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Specific heterologous F(ab')2 antibodies revert blood incoagulability resulting from envenoming by Lonomia obliqua caterpillars.

Rocha-Campos¹,

Gonçalves²,

Higashi³

et al. 2001

The American Journal of Tropical Medicine and Hygiene

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“…caterpillars have so far characterized two fibrinolytic proteins from L. achelous, named Achelase I and Achelase II (Amarant et al, 1991). The present study attempts to understand the molecular components likely involved in the envenomation by L. obliqua.…”

Section: Resultsmentioning

confidence: 96%

“…Some of the active principles produced by Lonomia sp. that interfere with the hemostatic system have been characterized: fibrinolytic proteases in the hemolymph of L. achelous (Amarant et al, 1991), prothrombin or factor X activators in L. obliqua bristle (Donato et al, 1998) and α-fibrinogenases found in both bristles and in a secretion obtained after freezing L. obliqua caterpillars (Veiga et al, 2003;Pinto et al, 2004). Other active compounds such as phospholipases were also described in Lonomia sp.…”

Section: Introductionmentioning

confidence: 99%

“…In fact, only partial amino acid sequences of two fibrinolytic proteases from L. achelous have been reported before (Amarant et al, 1991). Furthermore, a GenBank search for " Lonomia", in November, 2004, revealed only the amino acid sequences of these two fibrinogenases and the sequence of polyhedrin, a multiple nucleopolyhedrovirus from L. obliqua.…”

Section: Introductionmentioning

confidence: 99%

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A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: Identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome

Veiga

Ribeiro

Guimarães

et al. 2005

Gene

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Accidents with the caterpillar Lonomia obliqua are often associated with a coagulation disorder and hemorrhagic syndrome in humans. In the present study, we have constructed cDNA libraries from two venomous structures of the caterpillar, namely the tegument and the bristle. Highthroughput sequencing and bioinformatics analyses were performed in parallel. Over one thousand cDNAs were obtained and clustered to produce a database of 538 contigs and singletons (clusters) for the tegument library and 368 for the bristle library. We have thus identified dozens of fulllength cDNAs coding for proteins with sequence homology to snake venom prothrombin activator, trypsin-like enzymes, blood coagulation factors and prophenoloxidase cascade activators. We also report cDNA coding for cysteine proteases, Group III phospholipase A2, Ctype lectins, lipocalins, in addition to protease inhibitors including serpins, Kazal-type inhibitors, cystatins and trypsin inhibitor-like molecules. Antibacterial proteins and housekeeping genes are also described. A significant number of sequences were devoid of database matches, suggesting that their biologic function remains to be defined. We also report the N-terminus of the most abundant proteins present in the bristle, tegument, hemolymph, and "cryosecretion". Thus, we have created a catalog that contains the predicted molecular weight, isoelectric point, accession number, and putative function for each selected molecule from the venomous structures of L. obliqua. The role of these molecules in the coagulation disorder and hemorrhagic syndrome caused by envenomation with this caterpillar is discussed. All sequence information and the Supplemental Data, including Figures and Tables with hyperlinks to FASTA-formatted files for each contig and the best match to the Databases, are available at http://www.ncbi.nih.gov/projects/omes.

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Moths and Butterflies (Order: Lepidoptera)

Barceloux

2008

Medical Toxicology of Natural Substances

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Isolation and complete amino acid sequence of two fibrinolytic proteinases from the toxic Saturnid caterpillar Lonomia achelous

Cited by 56 publications

References 15 publications

Specific heterologous F(ab')2 antibodies revert blood incoagulability resulting from envenoming by Lonomia obliqua caterpillars.

Specific heterologous F(ab')2 antibodies revert blood incoagulability resulting from envenoming by Lonomia obliqua caterpillars.

A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: Identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome

Moths and Butterflies (Order: Lepidoptera)

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