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1.
J Econ Entomol ; 108(4): 1961-71, 2015 Aug.
Article in English | MEDLINE | ID: mdl-26470341

ABSTRACT

Linepithema humile (Mayr), the Argentine ant, is an invasive pest that has spread throughout the United States and is a problem in natural and managed habitats in South Carolina. Foraging patterns and the effectiveness of liquid baits for control of this pest have been studied in urban areas. However, similar studies have not been conducted in natural areas such as parks, picnic grounds, or campsites. L. humile populations can be large and widespread, making them a major nuisance pest for visitors to these natural areas. The primary objective of this study was to determine an effective distance between bait stations for control of L. humile in a natural area. A double antibody-sandwich enzyme-linked immunosorbent assay (DAS-ELISA) procedure was used to detect individual ants that consumed rabbit immunoglobin (IgG) protein for marking and tracking. In both lab and field conditions, there was a significant difference in the detection of IgG in ants fed protein marker mixed with sugar water compared with ants only fed sugar water. Additional field studies revealed that an individual ant could retain detectable levels of protein marker for 3 d and that an ant feeding on IgG containing bait could be detected over 15 m from the original bait source. Overall, we found that using liquid ant baits, with a placement of 20 m between stations, was effective in reducing L. humile numbers between April to October, 2012 in a natural park area of Lake Greenwood State Park, SC.


Subject(s)
Ants/physiology , Insect Control/methods , Animals , Appetitive Behavior , Enzyme-Linked Immunosorbent Assay , Parks, Recreational , South Carolina
2.
Arch Virol ; 159(10): 2791-3, 2014 Oct.
Article in English | MEDLINE | ID: mdl-24838850

ABSTRACT

The complete genomic sequence of Cassava Ivorian bacilliform virus (CIBV) is described. The virus has a genomic organization similar to that of pelargonium zonate spot virus (PZSV), the type member of the genus Anulavirus, but it is most closely related to a second, recently described, anulavirus, Amazon lily mild mottle virus (ALiMMV).


Subject(s)
Bromoviridae/classification , Bromoviridae/genetics , Genome, Viral/genetics , Manihot/virology , Amino Acid Sequence , Base Sequence , Genetic Variation , Molecular Sequence Data , Open Reading Frames/genetics , Plant Diseases/virology , RNA, Viral/genetics , Sequence Analysis, RNA , Viral Proteins/genetics
3.
Adv Virus Res ; 87: 139-81, 2013.
Article in English | MEDLINE | ID: mdl-23809923

ABSTRACT

Ilarviruses were among the first 16 groups of plant viruses approved by ICTV. Like Alfalfa mosaic virus (AMV), bromoviruses, and cucumoviruses they are isometric viruses and possess a single-stranded, tripartite RNA genome. However, unlike these other three groups, ilarviruses were recognized as being recalcitrant subjects for research (their ready lability is reflected in the sigla used to create the group name) and were renowned as unpromising subjects for the production of antisera. However, it was recognized that they shared properties with AMV when the phenomenon of genome activation, in which the coat protein (CP) of the virus is required to be present to initiate infection, was demonstrated to cross group boundaries. The CP of AMV could activate the genome of an ilarvirus and vice versa. Development of the molecular information for ilarviruses lagged behind the knowledge available for the more extensively studied AMV, bromoviruses, and cucumoviruses. In the past 20 years, genomic data for most known ilarviruses have been developed facilitating their detection and allowing the factors involved in the molecular biology of the genus to be investigated. Much information has been obtained using Prunus necrotic ringspot virus and the more extensively studied AMV. A relationship between some ilarviruses and the cucumoviruses has been defined with the recognition that members of both genera encode a 2b protein involved in RNA silencing and long distance viral movement. Here, we present a review of the current knowledge of both the taxonomy and the molecular biology of this genus of agronomically and horticulturally important viruses.


Subject(s)
Genome, Viral , Host-Pathogen Interactions/immunology , Ilarvirus , RNA, Viral/genetics , Amino Acid Sequence , Genetic Variation , Ilarvirus/classification , Ilarvirus/genetics , Ilarvirus/metabolism , Plants/virology , RNA-Binding Proteins , Sequence Alignment , Viral Proteins/chemistry , Viral Proteins/genetics , Virion/metabolism , Virion/physiology
4.
Arch Virol ; 153(11): 2169-72, 2008.
Article in English | MEDLINE | ID: mdl-18972183

ABSTRACT

Partial sequences of the RNA 1 and RNA 2 of LRMV are described. These confirm that LRMV is most closely related to members of the subgroup 2 ilarviruses. However, these sequences also show that LRMV is sufficiently different from other members of subgroup 2 so as to explain why oligonucleotide primers that had been used to amplify related subgroup 2 viruses did not amplify corresponding products from LRMV.


Subject(s)
Ilarvirus/classification , Ilarvirus/genetics , RNA, Viral/genetics , Amino Acid Sequence , Base Sequence , Molecular Sequence Data , Open Reading Frames , Sequence Alignment
5.
Virus Res ; 90(1-2): 217-24, 2002 Dec.
Article in English | MEDLINE | ID: mdl-12457976

ABSTRACT

Complete nucleotide sequences were determined for the four dsRNA segments present in isolate 247 of Discula destructiva from South Carolina. The largest dsRNA (dsRNA 1) was 1787 bp in length with a single open reading frame (ORF) that coded for a putative RNA-dependent RNA polymerase (RdRp). The dsRNA 2 was 1585 bp in length with a single ORF that coded for a putative viral coat protein. Both the dsRNA 3 (1178 bp in length) and dsRNA 4 (308 bp) contained single ORFs. However, neither the nucleotide sequence nor the sequence of the putative translation products, showed any similarity with sequences currently available from GenBank. Although distinct, all 4 dsRNAs showed conserved nucleotides at both the 5' and 3' termini. Sequences of the two dsRNAs in an isolate of D. destructiva (331 originating from Idaho) were similar in length to, and shared similarity with, the dsRNA 1 and dsRNA 2 of isolate 247. However, although the putative RdRps of isolates 247 and 331 are closely related, the putative viral coat proteins coded for by the respective dsRNA 2s are distinct. Thus, the dsRNAs in the two fungal isolates appeared to originate from distinct, but related viruses, which we have named D. destructiva virus 1 and D. destructiva virus 2, respectively. Phylogenetic analysis indicated that the two viruses were most closely related to Fusarium solani virus 1 and should be considered members of the genus Partitivirus. Another isolate of D. destructiva (272.1) contains a 12 kb dsRNA in addition to the 4 dsRNAs found in isolate 247. Partial sequence of this 12 kb molecule showed a relationship to other large dsRNA molecules isolated from plants.


Subject(s)
Ascomycota/virology , Genome, Viral , RNA Viruses/genetics , RNA, Double-Stranded/genetics , Sequence Analysis, DNA , Amino Acid Sequence , Capsid Proteins/chemistry , Capsid Proteins/genetics , Cornus/microbiology , Molecular Sequence Data , Plant Diseases/microbiology , RNA Viruses/isolation & purification , RNA, Viral/genetics , RNA-Dependent RNA Polymerase/chemistry , RNA-Dependent RNA Polymerase/genetics
6.
J Gen Virol ; 83(Pt 6): 1477-1482, 2002 Jun.
Article in English | MEDLINE | ID: mdl-12029163

ABSTRACT

The complete nucleotide sequences of genomic segments S1, S3 and S4 from Bombyx mori cypovirus 1 (BmCPV-1) have been determined. The segments consisted of 4190, 3846 and 3262 nucleotides encoding putative proteins of 1333, 1239 and 1058 amino acids with molecular masses of approximately 148, 140 and 120 kDa (p148, p140 and p120, respectively). All segments possess a single open reading frame. Homology searches showed that all three proteins have homologies to proteins of Rice ragged stunt virus, a member of the genus Oryzavirus within the family REOVIRIDAE: Partial homologies of p140 to structural proteins in other viruses were also found. The predicted molecular masses and the homologies with structural proteins in other viruses lead us to suggest that S1, S3 and S4 encode the capsid proteins VP1, VP3, and VP4, respectively, of BmCPV-1.


Subject(s)
Bombyx/virology , Capsid/genetics , Genome, Viral , Reoviridae/genetics , Amino Acid Sequence , Animals , Cloning, Molecular , Molecular Sequence Data , Open Reading Frames , Reoviridae/chemistry , Sequence Alignment , Sequence Homology, Amino Acid
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