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No. de sistema: 000060438

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008 _ _ 200518m20199999xx^^r^p^o^^^^z0^^^a0eng^d
040 _ _ a| ECO
c| ECO
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245 0 0 a| Biochemical and functional characterization of glycoside hydrolase family 16 genes in Aedes aegypti larvae
b| identification of the major digestive ß-1,3-Glucanase
506 _ _ a| Acceso en línea sin restricciones
520 1 _ a| Insect β-1,3-glucanases belong to Glycoside Hydrolase Family 16 (GHF16) and are involved in digestion of detritus and plant hemicellulose. In this work, we investigated the role of GHF16 genes in Aedes aegypti larvae, due to their detritivore diet. Aedes aegypti genome has six genes belonging to GHF16 (Aae GH16.1 – Aae GH16.6), containing two to six exons. Sequence analysis suggests that five of these GHF16 sequences (Aae GH16.1, 2, 3, 5, and 6) contain the conserved catalytic residues of this family and correspond to glucanases. All genomes of Nematocera analyzed showed putative gene duplications corresponding to these sequences. Aae GH16.4 has no conserved catalytic residues and is probably a β-1,3-glucan binding protein involved in the activation of innate immune responses. Additionally, Ae. aegypti larvae contain significant β-1,3-glucanase activities in the head, gut and rest of body. These activities have optimum pH about 5–6 and molecular masses between 41 and 150 kDa. All GHF16 genes above showed different levels of expression in the larval head, gut or rest ofthebody. Knock-down of AeGH16.5 resulted in survival and pupation rates lower than controls (dsGFP and water treated). However, under stress conditions, severe mortalities were observed in AeGH16.1 and AeGH16.6 knocked-down larvae. Enzymatic assays of β-1,3-glucanase in AeGH16.5 silenced larvae exhibited lower activity in the gut and no change in the rest of the body. Chromatographic activity profiles from gut samples after GH16.5 silencing showed suppression of enzymatic activity, suggesting that this gene codes for the digestive larval β-1,3-glucanase of Ae. aegypti. This gene and enzyme are attractive targets for new control strategies, based on the impairment of normal gut physiology.
530 _ _ a| Disponible en línea
533 _ _ a| Reproducción electrónica en formato PDF
538 _ _ a| Adobe Acrobat profesional 6.0 o superior
650 _ 4 a| Aedes aegypti
650 _ 4 a| Larvas de insectos
650 _ 4 a| Glicosidasas
650 _ 4 a| Filogenética
650 _ 4 a| Control de vectores
700 1 _ a| Santos Souza, Raquel
e| autora
700 1 _ a| Faria Gama, Maiara do Valle
e| autora
700 1 _ a| Schama, Renata
e| autora
700 1 _ a| Pereira Lima, José Bento
e| autor
700 1 _ a| Díaz Albíter, Héctor Manuel
c| Doctor
e| autor
700 1 _ a| Ariel Genta, Fernando
e| autor
773 0 _
t| Frontiers in Physiology
g| Volume 10, artículo 122 (February 2019), p. 1-16
x| 1664-042X
856 4 1 u| https://www.frontiersin.org/articles/10.3389/fphys.2019.00122/full
z| Artículo electrónico
902 _ _ a| BG / MM
904 _ _ a| Mayo 2020
905 _ _ a| Artecosur
905 _ _ a| Biblioelectrónica
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Biochemical and functional characterization of glycoside hydrolase family 16 genes in Aedes aegypti larvae: identification of the major digestive ß-1,3-Glucanase
Santos Souza, Raquel (autora)
Faria Gama, Maiara do Valle (autora)
Schama, Renata (autora)
Pereira Lima, José Bento (autor)
Díaz Albíter, Héctor Manuel (autor)
Ariel Genta, Fernando (autor)
Nota: Disponible en línea
Acceso en línea sin restricciones
Contenido en: Frontiers in Physiology. Volume 10, artículo 122 (February 2019), p. 1-16. ISSN: 1664-042X
No. de sistema: 60438
Tipo: Artículo
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Inglés

"Insect β-1,3-glucanases belong to Glycoside Hydrolase Family 16 (GHF16) and are involved in digestion of detritus and plant hemicellulose. In this work, we investigated the role of GHF16 genes in Aedes aegypti larvae, due to their detritivore diet. Aedes aegypti genome has six genes belonging to GHF16 (Aae GH16.1 – Aae GH16.6), containing two to six exons. Sequence analysis suggests that five of these GHF16 sequences (Aae GH16.1, 2, 3, 5, and 6) contain the conserved catalytic residues of this family and correspond to glucanases. All genomes of Nematocera analyzed showed putative gene duplications corresponding to these sequences. Aae GH16.4 has no conserved catalytic residues and is probably a β-1,3-glucan binding protein involved in the activation of innate immune responses. Additionally, Ae. aegypti larvae contain significant β-1,3-glucanase activities in the head, gut and rest of body. These activities have optimum pH about 5–6 and molecular masses between 41 and 150 kDa. All GHF16 genes above showed different levels of expression in the larval head, gut or rest ofthebody. Knock-down of AeGH16.5 resulted in survival and pupation rates lower than controls (dsGFP and water treated). However, under stress conditions, severe mortalities were observed in AeGH16.1 and AeGH16.6 knocked-down larvae. Enzymatic assays of β-1,3-glucanase in AeGH16.5 silenced larvae exhibited lower activity in the gut and no change in the rest of the body. Chromatographic activity profiles from gut samples after GH16.5 silencing showed suppression of enzymatic activity, suggesting that this gene codes for the digestive larval β-1,3-glucanase of Ae. aegypti. This gene and enzyme are attractive targets for new control strategies, based on the impairment of normal gut physiology."


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