MipLAAO, a new L-amino acid oxidase from the redtail coral snake, Micrurus mipartitus

 

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Detalles Bibliográficos
Autores: Rey Suárez, Paola, Acosta, Cristian, Torres Lamus, Uday Daniel, Saldarriaga Córdoba, Mónica María, Lomonte, Bruno, Núñez Rangel, Vitelbina
Formato: artículo original
Fecha de Publicación:2018
Descripción:L-amino acid oxidases (LAAOs) are ubiquitous enzymes in nature. Bioactivities described for these enzymes include apoptosis induction, edema formation, induction or inhibition of platelet aggregation, as well as antiviral, antiparasite, and antibacterial actions. With over 80 species, Micrurus snakes are the representatives of the Elapidae family in the New World. Although LAAOs in Micrurus venoms have been predicted by venom gland transcriptomic studies and detected in proteomic studies, no enzymes of this kind have been previously purified from their venoms. Earlier proteomic studies revealed that the venom of M. mipartitus from Colombia contains 4% of LAAO. This enzyme, here named MipLAAO, was isolated and biochemically and functionally characterized. The enzyme is found in monomeric form, with an isotope-averaged molecular mass of 59,100.6 Da, as determined by MALDI-TOF. Its oxidase activity shows substrate preference for hydrophobic amino acids, being optimal at pH 8.0. By nucleotide sequencing of venom gland cDNA of mRNA transcripts obtained from a single snake, six isoforms of MipLAAO with minor variations among them were retrieved. The deduced sequences present a mature chain of 483 amino acids, with a predicted pI of 8.9, and theoretical masses between 55,010.9 and 55,121.0 Da. The difference with experimentally observed mass is likely due to glycosylation, in agreement with the finding of three putative N-glycosylation sites in its amino acid sequence. A phylogenetic analysis of MmipLAAO placed this new enzyme within the clade of homologous proteins from elapid snakes, characterized by the conserved Serine at position 223, in contrast to LAAOs from viperids. MmipLAAO showed a potent bactericidal effect on S. aureus (MIC: 2 mg/mL), but not on E. coli. The former activity could be of interest to future studies assessing its potential as antimicrobial agent.
País:Kérwá
Institución:Universidad de Costa Rica
Repositorio:Kérwá
OAI Identifier:oai:https://www.kerwa.ucr.ac.cr:10669/76539
Acceso en línea:https://peerj.com/articles/4924/
https://hdl.handle.net/10669/76539
Access Level:acceso abierto
Palabra clave:Antibacterial activity
L-Aminoacid oxidase
Escherichia coli
Staphyloccocus aureus
Micrurus mipartitus
Snake venom
Protein sequence
Coral snake
615.946 Venenos animales