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ARS Home » Southeast Area » Gainesville, Florida » Center for Medical, Agricultural and Veterinary Entomology » Imported Fire Ant and Household Insects Research » Research » Publications at this Location » Publication #278056
Title: Confirmation of the genome position and mass of the viral protien, VP3, of Solenopsis Invicta Virus 1 (Picornavirales: Dicistroviridae) infecting the Red Imported Fire Ant (Hymenoptera: Formicidae)

Author
item Valles, Steven
item Strong, Charles

Submitted to: Florida Entomologist
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/23/2012
Publication Date: 6/1/2012
Citation: Valles, S.M., Strong, C.A. 2012. Confirmation of the genome position and mass of the viral protien, VP3, of Solenopsis Invicta Virus 1 (Picornavirales: Dicistroviridae) infecting the Red Imported Fire Ant (Hymenoptera: Formicidae). Florida Entomologist. 95(2):494-496.

Interpretive Summary: The red imported fire ant is an invasive insect pest that currently infests about 300 million acres and causes economic losses that exceed 6 billion dollars annually in the United States. Solenopsis invicta virus 1 is the first virus discovered from the red imported fire ant. This virus may find utility as a biopesticide to naturally control this ant. In order to develop this virus as a biopesticide, knowledge of the biology of the virus must be understood. In an effort to advance our understanding of the infection process of SINV-1, scientists at the USDA-ARS, Center for Medical, Agricultural and Veterinary Entomology (Gainesville, FL) have examined SINV-1-infected fire ant colonies for the production of capsid proteins. These results advance our knowledge of the virus infection process.

Technical Abstract: A predicted peptide sequence corresponding to the capsid protein VP3 of SINV-1 was used to prepare a polyclonal antibody preparation and probe SDS-PAGE separated proteins from SINV-1 particles and S. invicta ants. The SINV-1 VP3 antibody preparation recognized a 24 kDa protein from denatured SINV-1 particles and from SINV-1-infected worker ants confirming VP3 synthesis, genome position, and mass. While detection of the unprocessed ORF 2 polyprotein (molecular mass of 126 kDa) was anticipated, a protein of this mass was not observed. Epitope availability, antibody detection limitations, and inactive periods of viral replication may explain failure to detect the unprocessed polyprotein. In conclusion, we provide further empirical evidence for the production of VP3 from SINV-1 ORF 2, as well as confirmation of the genome position of this capsid protein.