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...
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| Format: | Artículo |
| Language: | Inglés |
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Springer
2018
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| Online Access: | https://link.springer.com/article/10.1007%2Fs11262-013-1019-7 http://hdl.handle.net/20.500.12123/3553 https://doi.org/10.1007/s11262-013-1019-7 |
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| author | Salvador, Ricardo Ferrelli, Maria Leticia Sciocco, Alicia Ines Romanowski, Victor |
| author_browse | Ferrelli, Maria Leticia Romanowski, Victor Salvador, Ricardo Sciocco, Alicia Ines |
| author_facet | Salvador, Ricardo Ferrelli, Maria Leticia Sciocco, Alicia Ines Romanowski, Victor |
| author_sort | Salvador, Ricardo |
| collection | INTA Digital |
| 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 | Artículo |
| id | INTA3553 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2018 |
| publishDateRange | 2018 |
| publishDateSort | 2018 |
| publisher | Springer |
| publisherStr | Springer |
| record_format | dspace |
| spelling | INTA35532018-10-03T16:28:08Z Analysis of a chitinase from EpapGV, a fast killing betabaculovirus Salvador, Ricardo Ferrelli, Maria Leticia Sciocco, Alicia Ines Romanowski, Victor Baculovirus Quitinasa Betabaculovirus Epinotia aporema Identificación Chitinase Identification 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. Instituto de Microbiología y Zoología Agrícola Fil: Salvador, Ricardo. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina Fil: Ferrelli, Maria Leticia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina Fil: Sciocco, Alicia Ines. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Microbiología y Zoología Agrícola; Argentina Fil: Romanowski, Victor. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Biotecnología y Biología Molecular. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Instituto de Biotecnología y Biología Molecular; Argentina 2018-10-03T15:35:39Z 2018-10-03T15:35:39Z 2014-04 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion https://link.springer.com/article/10.1007%2Fs11262-013-1019-7 http://hdl.handle.net/20.500.12123/3553 0920-8569 1572-994X https://doi.org/10.1007/s11262-013-1019-7 eng info:eu-repo/semantics/restrictedAccess application/pdf Springer Virus Genes 48 (2) : 406–409 (April 2014) |
| spellingShingle | Baculovirus Quitinasa Betabaculovirus Epinotia aporema Identificación Chitinase Identification Salvador, Ricardo Ferrelli, Maria Leticia Sciocco, Alicia Ines Romanowski, Victor Analysis of a chitinase from EpapGV, a fast killing betabaculovirus |
| title | 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_short | Analysis of a chitinase from EpapGV, a fast killing betabaculovirus |
| title_sort | analysis of a chitinase from epapgv a fast killing betabaculovirus |
| topic | Baculovirus Quitinasa Betabaculovirus Epinotia aporema Identificación Chitinase Identification |
| url | https://link.springer.com/article/10.1007%2Fs11262-013-1019-7 http://hdl.handle.net/20.500.12123/3553 https://doi.org/10.1007/s11262-013-1019-7 |
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