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Title: Functional characterization of Autographa californica multiple nucleopolyhedrovirus gp16 (ac130)

Abstract

To investigate the function of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) gp16, multiple gp16-knockout and repair mutants were constructed and characterized. No obvious difference in productivity of budded virus, DNA synthesis, late gene expression and morphogenesis was observed between gp16-knockout and repair viruses, but gp16 deletion resulted in six hours of lengthening in ST{sub 50} to the third instar Spodoptera exigua larvae in bioassays. GP16 was fractionated mainly in the light membrane fraction, by subcellular fractionation. A GP16-EGFP fusion protein was predominantly localized close around the nuclear membrane in infected cells, being coincident with formation of the vesicles associated with the nuclear membrane, which hosted nucleocapsids released from the nucleus. These data suggest that gp16 is not required for viral replication, but may be involved in membrane trafficking associated with the envelopment/de-envelopment of budded viruses when they cross over the nuclear membrane and pass through cytoplasm. - Highlights: • gp16 knockout and repair mutants of AcMNPV were constructed and characterized. • AcMNPV gp16 is not essential to virus replication. • Deletion of gp16 resulted in time lengthening to kill S. exigua larvae. • GP16 was localized close around the nuclear membrane of infected cells. • GP16 was fractionated in the lightmore » membrane fraction in subcellular fractionation.« less

Authors:
; ; ;
Publication Date:
OSTI Identifier:
22435057
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 464-465; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACIDS; BIOASSAY; BIOLOGICAL REPAIR; CELL NUCLEI; CYTOPLASM; DNA; GENES; HOST; LARVAE; MEMBRANES; MORPHOGENESIS; MUTANTS; PROTEINS; SYNTHESIS; VIRUSES

Citation Formats

Yang, Ming, Huang, Cui, Qian, Duo-Duo, and Li, Lu-Lin. Functional characterization of Autographa californica multiple nucleopolyhedrovirus gp16 (ac130). United States: N. p., 2014. Web. doi:10.1016/J.VIROL.2014.07.030.
Yang, Ming, Huang, Cui, Qian, Duo-Duo, & Li, Lu-Lin. Functional characterization of Autographa californica multiple nucleopolyhedrovirus gp16 (ac130). United States. https://doi.org/10.1016/J.VIROL.2014.07.030
Yang, Ming, Huang, Cui, Qian, Duo-Duo, and Li, Lu-Lin. 2014. "Functional characterization of Autographa californica multiple nucleopolyhedrovirus gp16 (ac130)". United States. https://doi.org/10.1016/J.VIROL.2014.07.030.
@article{osti_22435057,
title = {Functional characterization of Autographa californica multiple nucleopolyhedrovirus gp16 (ac130)},
author = {Yang, Ming and Huang, Cui and Qian, Duo-Duo and Li, Lu-Lin},
abstractNote = {To investigate the function of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) gp16, multiple gp16-knockout and repair mutants were constructed and characterized. No obvious difference in productivity of budded virus, DNA synthesis, late gene expression and morphogenesis was observed between gp16-knockout and repair viruses, but gp16 deletion resulted in six hours of lengthening in ST{sub 50} to the third instar Spodoptera exigua larvae in bioassays. GP16 was fractionated mainly in the light membrane fraction, by subcellular fractionation. A GP16-EGFP fusion protein was predominantly localized close around the nuclear membrane in infected cells, being coincident with formation of the vesicles associated with the nuclear membrane, which hosted nucleocapsids released from the nucleus. These data suggest that gp16 is not required for viral replication, but may be involved in membrane trafficking associated with the envelopment/de-envelopment of budded viruses when they cross over the nuclear membrane and pass through cytoplasm. - Highlights: • gp16 knockout and repair mutants of AcMNPV were constructed and characterized. • AcMNPV gp16 is not essential to virus replication. • Deletion of gp16 resulted in time lengthening to kill S. exigua larvae. • GP16 was localized close around the nuclear membrane of infected cells. • GP16 was fractionated in the light membrane fraction in subcellular fractionation.},
doi = {10.1016/J.VIROL.2014.07.030},
url = {https://www.osti.gov/biblio/22435057}, journal = {Virology},
issn = {0042-6822},
number = ,
volume = 464-465,
place = {United States},
year = {Mon Sep 15 00:00:00 EDT 2014},
month = {Mon Sep 15 00:00:00 EDT 2014}
}