Analysis of a chitinase from EpapGV, a fast killing betabaculovirus

The main function of baculoviral chitinase protein (V-CHIA) is to promote the final liquefaction of infected host larvae, facilitating the dispersion of occlusion bodies (OBs) in the environment. In this study, a v-chiA from Epinotia aporema Granulovirus (EpapGV) was identified and characterized. Th...

Descripción completa

Guardado en:
Detalles Bibliográficos
Autores principales: Salvador, Ricardo, Ferrelli, María Leticia, Sciocco Cap, Alicia, Romanowski, Víctor
Formato: Articulo
Lenguaje:Inglés
Publicado: 2013
Materias:
Biología
V-CHIA
Baculovirus
EpapGV
Chitinase
Peritrophic membrane
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/143191
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-143191
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Biología
V-CHIA
Baculovirus
EpapGV
Chitinase
Peritrophic membrane
spellingShingle Biología
V-CHIA
Baculovirus
EpapGV
Chitinase
Peritrophic membrane
Salvador, Ricardo
Ferrelli, María Leticia
Sciocco Cap, Alicia
Romanowski, Víctor
Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
topic_facet Biología
V-CHIA
Baculovirus
EpapGV
Chitinase
Peritrophic membrane
description The main function of baculoviral chitinase protein (V-CHIA) is to promote the final liquefaction of infected host larvae, facilitating the dispersion of occlusion bodies (OBs) in the environment. In this study, a v-chiA from Epinotia aporema Granulovirus (EpapGV) was identified and characterized. The 1,713 base pairs long open reading frame encodes a protein of 570 amino acids with a predicted molecular weight of 63 kDa. EpapGV V-CHIA sequence alignment resulted 62 % identical to Pieris rapae GV and Blastp search revealed a high conservation among all baculovirus chitinases. Amino acid sequence analysis indicated that the C-terminal KDEL present in most alphabaculovirus chitinases is absent in EpapGV V-CHIA, as well as in the rest of the betabaculoviruses. Phylogenetic analysis was performed with bacterial, lepidopteran, and baculoviral chitinase sequences available in databases. Using an AcMNPV bacmid (bApGOZA) a recombinant Ac-chiAEpapGV was obtained in order to overexpress EpapGV V-CHIA in cell culture. The presence of chitinase was detected in purified AcMNPV-chiAEpapGV OBs. Peritrophic membranes of Anticarsia gemmatalis larvae fed with recombinant OBs showed an altered structure. The results presented in this study show that EpapGV chitinase overexpression in recombinant baculovirus can cause association of this protein with OBs, and suggest that this could be used to evaluate the protein role in early stages of baculoviral infections.
format Articulo
Articulo
author Salvador, Ricardo
Ferrelli, María Leticia
Sciocco Cap, Alicia
Romanowski, Víctor
author_facet Salvador, Ricardo
Ferrelli, María Leticia
Sciocco Cap, Alicia
Romanowski, Víctor
author_sort Salvador, Ricardo
title Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
title_short Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
title_full Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
title_fullStr Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
title_full_unstemmed Analysis of a chitinase from EpapGV, a fast killing betabaculovirus
title_sort analysis of a chitinase from epapgv, a fast killing betabaculovirus
publishDate 2013
url http://sedici.unlp.edu.ar/handle/10915/143191
work_keys_str_mv AT salvadorricardo analysisofachitinasefromepapgvafastkillingbetabaculovirus
AT ferrellimarialeticia analysisofachitinasefromepapgvafastkillingbetabaculovirus
AT scioccocapalicia analysisofachitinasefromepapgvafastkillingbetabaculovirus
AT romanowskivictor analysisofachitinasefromepapgvafastkillingbetabaculovirus
bdutipo_str Repositorios
_version_ 1764820459666276356

Ejemplares similares