A peptide with similarity to baculovirus ODV-E66 binds the gut epithelium of Heliothis virescens and impedes infection with Autographa californica multiple nucleopolyhedrovirus
Department of Entomology, Iowa State University, Ames, IA 50011, USA.Journal of General Virology (Impact Factor: 3.18). 04/2011; 92(Pt 5):1051-60. DOI: 10.1099/vir.0.028118-0
Baculoviruses infect their lepidopteran hosts via the midgut epithelium through binding of occlusion-derived virus (ODV) and fusion between the virus envelope and microvillar membranes. To identify genes and sequences that are involved in this process, a random phage display library was screened for peptides that bound to brush border membrane vesicles (BBMV) derived from the midgut epithelium of Heliothis virescens. Seventeen peptides that bound to BBMV were recovered. Two of these, HV1 and HV2, had sequence similarity to the ODV envelope protein ODV-E66 that is found in five species of alphabaculoviruses. Chemically synthesized versions of HV1 and HV2, and two peptides (AcE66A and AcE66B) derived from similar sequences of Autographa californica multiple nucleopolyhedrovirus (AcMNPV) ODV-E66, bound to unfixed cryosections of whole midgut tissues. AcE66A, but not HV1, bound to H. virescens gut BBMV proteins on a far-Western blot. Competition assays with HV1 and purified AcMNPV ODV resulted in decreased mortality of H. virescens larvae at a dose of 1 LD(50), and a significant increase in survival time at higher virus concentrations. These results suggest a role for ODV-E66 in baculovirus infection of lepidopteran larval midgut epithelium.
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- "The understanding of the molecular determinants of plant virus–vector interactions allows the development of novel ways to control viruses by interfering with the initial steps in the interaction. Disruption of the acquisition process renders insects incapable of transmitting the virus or greatly reduces transmission efficiency and, thus, stops the transmission cycle (Liu et al. 2010; Shao et al. 2003; Sparks et al. 2011). In the case of TSWV, it was shown that one of the virus glycoproteins, G N , serves as the attachment protein of the virus (Whitfield et al. 2004). "
ABSTRACT: Vector-borne viruses are a threat to human, animal and plant health worldwide requiring the development of novel strategies for their control. Tomato spotted wilt virus (TSWV) is one of the ten most economically significant plant viruses and, together with other tospoviruses, is a threat to global food security. TSWV is transmitted by thrips, including the western flower thrips, Frankliniella occidentalis. Previously, we demonstrated that the TSWV glycoprotein GN binds to thrips vector midguts. We report here the development of transgenic plants that interfere with TSWV acquisition and transmission by the insect vector. Tomato plants expressing GN-S protein supported virus accumulation and symptom expression comparable to non-transgenic plants. However, virus titers in larval insects exposed to the infected transgenic plants were 3-log lower than insects exposed to infected non-transgenic control plants. The negative effect of the GN-S transgenics on insect virus titers persisted to adulthood, as evidenced by 4-log lower virus titers in adults and an average reduction of 87% in transmission efficiencies. These results demonstrate that an initial reduction in virus infection of the insect can result in a significant decrease in virus titer and transmission over the life-span of the vector, supportive of a dose-dependent relationship in the virus-vector interaction. These findings demonstrate that plant expression of a viral protein can be an effective way to block virus transmission by insect vectors.Molecular Plant-Microbe Interactions 01/2014; 27(3). DOI:10.1094/MPMI-09-13-0287-FI · 3.94 Impact Factor
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- "Finally, the data presented in this study may offer new directions in antiviral strategies based on virus–host interactions. Potential strategies have been reviewed recently by Kariithi et al. (2012) and include blocking of the initial attachment of GpSGHV to the tsetse midgut receptors using either antibodies against envelope proteins or competing peptides as reported for Autographa californica multicapsid nucleopolyhedrovirus in Heliothis virescens (Sparks et al., 2011), GpSGHV-specific gene silencing using RNA interference, inhibition of GpSGHV DNA polymerase (ORF79) by commercially available drugs (Abd-Alla et al., 2011) and blocking of RGD-directed cell adhesion as has been demonstrated for adenovirus (Bai et al., 1993). "
ABSTRACT: The Glossina pallidipes salivary gland hypertrophy virus (GpSGHV) is a dsDNA virus with rod-shaped, enveloped virions. Its 190-kb genome contains 160 putative protein-coding open reading frames (ORFs). Here, structural components, protein composition and associated aspects of GpSGHV morphogenesis and cytopathology were investigated. Four morphologically distinct structures: nucleocapsid, tegument, envelope, and helical surface projections, were observed in purified GpSGHV virions by electron microscopy. Nucleocapsids were present in virogenic stroma within the nuclei of infected salivary gland cells, whereas enveloped virions were located in the cytoplasm. The cytoplasm of infected cells appeared disordered and the plasma membranes disintegrated. Treatment of virions with 1% Nonidet P-40 efficiently partitioned the virions into envelope and nucleocapsid fractions. The fractions were separated by 12% SDS-PAGE followed by in-gel trypsin digestion and analysis of the tryptic peptides by LC-MS/MS. Using the MaxQuant program with Andromeda as a database search engine, a total of forty-five viral proteins were identified. Of these, ten and fifteen were associated with the envelope and the nucleocapsid fractions respectively, while twenty were detected in both fractions, most likely representing tegument proteins. In addition, fifty-one host-derived proteins were identified in the proteome of the virus particle, thirteen of which were verified to be incorporated into the mature virion using a proteinase K protection assay. This study provides important information about GpSGHV biology and suggests options for development of future anti-GpSGHV strategies by interfering with virus-host interactions.Journal of General Virology 10/2012; 94(Pt_1). DOI:10.1099/vir.0.047423-0 · 3.18 Impact Factor
- Abstract Book of the 44th Annual Meeting of the Society for Invertebrate Pathology; 08/2011
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