Identification of Four Isoforms of Esterase-5A fromCulex quinquefasciatusSay
| Autor: | Margarita de la Luz Martínez Fierro, Adriana E. Flores-Suarez, Iram P. Rodriguez-Sanchez, María de Lourdes Garza-Rodríguez, Laura E. Martínez de Villarreal, Gabriela González Olvera, Eugenia Cisneros Gutierrez, Norma Cruz-Fierro, Rafael González-Alvarez, Gustavo Ponce-Garcia, Diana Cristina Pérez-Ibave, Yamili Contreras-Perera, Ivan Delgado-Enciso, Olga Karina Villanueva-Segura, Idalia Garza Veloz, Jorge Alberto Martínez Davila, Mayra A. Gómez-Govea |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Genetics Ecology Esterase Gene 030231 tropical medicine Intron Biology Esterase Amino acid 03 medical and health sciences Carboxylesterase Exon 030104 developmental biology 0302 clinical medicine chemistry Insect Science Complementary DNA parasitic diseases Agronomy and Crop Science Gene |
| Zdroj: | Southwestern Entomologist. 43:91-107 |
| ISSN: | 2162-2647 0147-1724 |
| Popis: | The southern house mosquito, Culex quinquefasciatus Say (Diptera: Culicidae), transmits pathogens and is one of the most important vectors of human disease. The carboxylesterase mosquito genes encoded esterase enzyme involved in the mechanism that provides resistance to insecticides. We amplified by RTPCR four alternative transcripts from the esterase gene not reported previously (A, B, C, and D) from Cx. quinquefasciatus larvae from Monterrey, N.L., northeastern Mexico. Through cDNA sequences, we predicted amino acid sequences used to model the three-dimensional structure of protein isoforms. We determined dN and dS ratios to identify evolutionary forces which lead the family. PCR products were obtained from 5A esterases (1839, 1898, 1894, and 1953 bp). The translation sequence of the PCR products showed polypeptides of 612, 473, 282, and 282 amino acids in length for isoforms A, B, C, and D, respectively. Three exons and two introns were obtained in the analyzed sequences. The study sequences were compared with those previously published showing 98.7, 98.5, 91.5, and 91.5% amino acid similarity for isoforms A, B, C, and D, respectively. The threedimensional models showed that only ORF-D had the three amino acids corresponding to the catalytic triad, while ORF-A and ORF-C lacked one or two of the three amino acids. Esterase genes are under purifying of selection; a clue the members are functional. The processes might be useful in monitoring evolutionary dynamics of known carboxylesterase genes and identifying new carboxylesterase splicing. |
| Databáze: | OpenAIRE |
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