Lopap, a prothrombin activator from <i>Lonomia obliqua</i> belonging to the lipocalin family: recombinant production, biochemical characterization and structure–function insights

Reis, Cleyson Valença; Andrade, Sofia; Ramos, Oscar Henrique Pereira; Ramos, Celso Raul Romero; Ho, Paulo Lee; Batista, Isabel de Fátima Correia; Chudzinski-Tavassi, Ana Marisa

doi:10.1042/bj20060325

Cited by 44 publications

(66 citation statements)

References 39 publications

(56 reference statements)

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“…The analysis shows that the internal peptide sequences matched with proteins known as hemolin from different species of lepidopters. BLAST searches against expressed sequence tag data corresponding to the previously constructed cDNA library (3,4) revealed the existence of a partial transcript (accession number CX816408) whose deduced amino acid sequence matches several tryptic peptides. The complete sequencing of this transcript revealed an open reading frame (ORF) of 1239 bp encoding 413 amino acid residues.…”

Section: Resultsmentioning

confidence: 99%

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Alvarez-Flores

Furlin

Ramos

et al. 2011

Journal of Biological Chemistry

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Envenoming by the contact of human skin with Lonomia obliqua caterpillars promotes a hemorrhagic syndrome characterized by a consumptive coagulopathy. Losac (Lonomia obliqua Stuart factor activator) is a component of the bristle of L. obliqua that is probably partially responsible for the observed syndrome because it activates factor X and is recognized by an effective antilonomic serum. Here we unveil the proteolytic activity of Losac and demonstrate the feasibility of its recombinant production. On the other hand, Losac has no homology to known proteases, but it can be inhibited by PMSF, a serine protease inhibitor. Instead, it shows closer homology to members of the hemolin family of proteins, a group of cell adhesion molecules. The recombinant protein (rLosac) shortened the coagulation time of normal and deficient plasmas, whereas it was ineffective in factor X-deficient plasma unless reconstituted with this protein. rLosac was able to activate factor X in a dose-and time-dependent manner but not ␥-carboxyglutamic acid domainless factor X. Moreover, phospholipids and calcium ions increased rLosac activity. Also, rLosac had no effect on fibrin or fibrinogen, indicating its specificity for blood coagulation activation. Linear double reciprocal plots indicate that rLosac follows a Michaelis-Menten kinetics. Cleavage of factor X by rLosac resulted in fragments that are compatible with those generated by RVV-X (a well known factor X activator). Together, our results validate Losac as the first protein from the hemolin family exhibiting procoagulant activity through selective proteolysis on coagulation factor X.

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Section: Resultsmentioning

confidence: 99%

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Alvarez-Flores

Furlin

Ramos

et al. 2011

Journal of Biological Chemistry

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“…Lonomia obliqua venom contains a number of lipocalin-scaffold variants (134,155), and one of these, named Lopap, has a unique serine protease-like activity that activates prothrombin (127). There are currently no reports of other lipocalin-scaffold derivations with protease activity.…”

Section: Lipocalinmentioning

confidence: 99%

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Fry

Roelants

Champagne

et al. 2009

Annu. Rev. Genom. Hum. Genet.

722

778

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Throughout evolution, numerous proteins have been convergently recruited into the venoms of various animals, including centipedes, cephalopods, cone snails, fish, insects (several independent venom systems), platypus, scorpions, shrews, spiders, toxicoferan reptiles (lizards and snakes), and sea anemones. The protein scaffolds utilized convergently have included AVIT/colipase/prokineticin, CAP, chitinase, cystatin, defensins, hyaluronidase, Kunitz, lectin, lipocalin, natriuretic peptide, peptidase S1, phospholipase A 2 , sphingomyelinase D, and SPRY. Many of these same venom protein types have also been convergently recruited for use in the hematophagous gland secretions of invertebrates (e.g., fleas, leeches, kissing bugs, mosquitoes, and ticks) and vertebrates (e.g., vampire bats). Here, we discuss a number of overarching structural, functional, and evolutionary generalities of the protein families from which these toxins have been frequently recruited and propose a revised and expanded working definition for venom. Given the large number of striking similarities between the protein compositions of conventional venoms and hematophagous secretions, we argue that the latter should also fall under the same definition. 483

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“…El veneno de estas especies causa similares efectos, pero el mecanismo estricto es diferente. El veneno de Lonomia oblicua tiene actividad procoagulante (9,10) , mientras que el veneno de Lonomia achelous tiene actividad procoagulante y anticoagulante.…”

Section: Figuraunclassified

Niña con erucismo hemorrágico por Lonomia spp. reporte de un caso

Peña-Vásquez

Vásquez-Paz

Vásquez-Becerra

et al. 2016

Rev Peru Med Exp Salud Publica

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RESUMENLos accidentes causados por las setas urticantes o venenosas de las orugas de lepidópteros, se conocen como erucismo. Estos accidentes se producen por el contacto accidental, especialmente por los niños, con las cerdas sobre el cuerpo del insecto, conectadas con glándulas venenosas. Los síntomas pueden ser locales o sistémicos, con presentaciones clínicas fatales. El accidente ocasionado por las orugas del género Lonomia spp. puede desencadenar síndromes hemorrágicos, constituyendo estos la forma más grave de erucismo. Se reporta el caso de una niña de 5 años, procedente del poblado de Villarondos, en la Amazonía del Perú, departamento de Huánuco, la cual incidentalmente se hinca con las cerdas de una oruga, cursando luego con anemia hemolítica, plaquetopenia y trastorno de la coagulación. El diagnóstico fue establecido por la anamnesis, cuadro clínico, exámenes de laboratorio y respuesta al suero antilonómico. Se discuten los aspectos clínicos, laboratoriales y terapéuticos de erucismo por Lonomia spp.Palabras clave: Erucismo, Lonomia spp, coagulación intravascular diseminada, trastorno de la coagulación (fuente: DeCS BIREME). HEMORRHAGIC ERUCISM DUE TO Lonomia spp. IN A GIRL:A CASE REPORT ABSTRACT Accidents caused by urticating or poisonous setae from lepidoptera caterpillars are known as erucism. These accidents are produced by accidental contact, especially in children, with bristles on the insect's body surface, connected to venom glands. Symptoms may be local or systemic, with deadly clinical presentations. The accident caused by Lonomia spp. caterpillars can trigger bleeding disorders, which is considered the most severe type of erucism. The case of a 5-year-old girl is reported. She was from the town of Villarondos, in the Peruvian Amazon, department of Huánuco, who accidentally knelt down on caterpillar bristles, and subsequently experienced hemolytic anemia, plateletopenia, and coagulation disorder. The diagnosis was made based on the medical history, clinical manifestation, laboratory examination results, and response to antilonomic serum. The clinical, laboratory, and therapeutic aspects of erucism due to Lonomia spp. are discussed.

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Lopap, a prothrombin activator from Lonomia obliqua belonging to the lipocalin family: recombinant production, biochemical characterization and structure–function insights

Cited by 44 publications

References 39 publications

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

Losac, the First Hemolin that Exhibits Procogulant Activity through Selective Factor X Proteolytic Activation

The Toxicogenomic Multiverse: Convergent Recruitment of Proteins Into Animal Venoms

Niña con erucismo hemorrágico por Lonomia spp. reporte de un caso

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