Listar Microbiología por autor "1b49fc63-5b5b-45fe-bfd2-a63ebfb5a82b"
Mostrando ítems 1-5 de 5
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Functional analysis of DM64, an antimyotoxic protein with immunoglobulin-like structure from Didelphis marsupialis serum
Rocha, Surza Lucia Gonçalves; Lomonte, Bruno; Neves Ferreira, Ana Gisele da Costa; Trugilho, Monique Ramos de Oliveira; Junqueira de Azevedo, Inácio de Loiola Meirelles; Ho, Paulo Lee; Domont, Gilberto B.; Gutiérrez, José María; Perales, Jonas (2002-12-11)Bothrops snake venoms are known to induce local tissue damage such as hemorrhage and myonecrosis. The opossum Didelphis marsupialis is resistant to these snake venoms and has natural venom inhibitors in its plasma. The aim ... -
Molecular architecture of the antiophidic protein DM64 and its binding specificity to myotoxin II from Bothrops asper venom
Silva Soares, Bárbara da; Rocha, Surza Lucia Gonçalves; Almeida Bastos, Viviane; Borges Lima, Diogo; Costa Carvalho, Paulo; Gozzo, Fabio Cesar; Demeler, Borries; Williams, Tayler L.; Arnold, Janelle; Henrickson, Amy; Jørgensen, Thomas J.D.; Souza, Tatiana de Arruda Campos Brasil de; Perales, Jonas; Valente, Richard H.; Lomonte, Bruno; Gomes Neto, Francisco; Neves Ferreira, Ana Gisele da Costa (2022)DM64 is a toxin-neutralizing serum glycoprotein isolated from Didelphis aurita, an ophiophagous marsupial naturally resistant to snake envenomation. This 64 kDa antitoxin targets myotoxic phospholipases A2, which account ... -
Novel catalytically-inactive PII metalloproteinases from a viperid snake venom with substitutions in the canonical zinc-binding motif
Camacho Umaña, Erika; Sanz, Libia; Escalante Muñoz, Teresa; Pérez, Alicia; Villalta Romero, Fabián; Lomonte, Bruno; Neves Ferreira, Ana Gisele da Costa; Feoli Grant, Andrés; Calvete Chornet, Juan José; Gutiérrez, José María; Rucavado Romero, Alexandra (2016-10-12)Snake venom metalloproteinases (SVMPs) play key biological roles in prey immobilization and digestion. The majority of these activities depend on the hydrolysis of relevant protein substrates in the tissues. Hereby, we ... -
Screening for target toxins of the antiophidic protein DM64 through a gel-based interactomics approach
Rocha, Surza Lucia Gonçalves; Neves Ferreira, Ana Gisele da Costa; Trugilho, Monique Ramos de Oliveira; Angulo Ugalde, Yamileth; Lomonte, Bruno; Valente, Richard H.; Domont, Gilberto B.; Perales, Jonas (2017-01)DM64 is a glycosylated protein with antivenomactivity isolated fromthe serum of the opossumDidelphis aurita. It binds non-covalently to myotoxins I (Asp49) and II (Lys49) from Bothrops asper venom and inhibits their myotoxic ... -
SDS‑induced hexameric oligomerization of myotoxin‑II from Bothrops asper assessed by sedimentation velocity and nuclear magnetic resonance
Henrickson, Amy; Montina, Tony; Hazendonk, Paul; Lomonte, Bruno; Neves Ferreira, Ana Gisele da Costa; Demeler, Borries (2023)We report the solution behavior, oligomerization state, and structural details of myotoxin-II purified from the venom of Bothrops asper in the presence and absence of sodium dodecyl sulfate (SDS) and multiple lipids, as ...