6533b7cffe1ef96bd12599b7
RESEARCH PRODUCT
The sf32 unique gene of Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV) is a non-essential gene that could be involved in nucleocapsid organization in occlusion-derived virions.
Gloria BarreraSalvador HerreroLaila GasmiInés BeperetMiguel López-ferberPrimitivo CaballeroPrimitivo CaballeroTrevor WilliamsOihane Simónsubject
GenotypevirusesScienceGenome ViralSpodopteraSpodopteraVirus ReplicationOcclusion-derived virionsRecombinant virusHomology (biology)VirusViral Proteins03 medical and health sciencesAnimalsNucleocapsidSpodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV)Gene030304 developmental biology0303 health sciencesGenes Essential[SDV.BA.MVSA]Life Sciences [q-bio]/Animal biology/Veterinary medicine and animal HealthMultidisciplinaryNucleocapsid organizationbiology030306 microbiologyfungiQVirionRbiology.organism_classificationVirologyNucleopolyhedroviruses3. Good healthViral replicationEssential geneLarvaDNA Viral[SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/VirologyMedicinesf32Homologous recombinationResearch Articledescription
A recombinant virus lacking the sf32 gene (Sf32null), unique to the Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV), was generated by homologous recombination from a bacmid comprising the complete viral genome (Sfbac). Transcriptional analysis revealed that sf32 is an early gene. Occlusion bodies (OBs) of Sf32null contained 62% more genomic DNA than viruses containing the sf32 gene, Sfbac and Sf32null-repair, although Sf32null DNA was three-fold less infective when injected in vivo. Sf32null OBs were 18% larger in diameter and contained 17% more nucleocapsids within ODVs than those of Sfbac. No significant differences were detected in OB pathogenicity (50% lethal concentration), speed-of-kill or budded virus production in vivo. In contrast, the production of OBs/larva was reduced by 39% in insects infected by Sf32null compared to those infected by Sfbac. The SF32 predicted protein sequence showed homology (25% identity, 44% similarity) to two adhesion proteins from Streptococcus pyogenes and a single N-mirystoylation site was predicted. We conclude that SF32 is a non-essential protein that could be involved in nucleocapsid organization during ODV assembly and occlusion, resulting in increased numbers of nucleocapsids within ODVs.
year | journal | country | edition | language |
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2013-10-30 | PLoS ONE |