scholarly journals Baculovirus infection triggers a positive phototactic response in caterpillars: a response to Dobson et al . (2015)

2015 ◽  
Vol 11 (10) ◽  
pp. 20150633 ◽  
Author(s):  
Stineke van Houte ◽  
Monique M. van Oers ◽  
Yue Han ◽  
Just M. Vlak ◽  
Vera I. D. Ros
Keyword(s):  
Phototactic Response ◽  
Baculovirus Infection

scholarly journals Baculovirus infection triggers a positive phototactic response in caterpillars to induce ‘tree-top’ disease

2014 ◽  
Vol 10 (12) ◽  
pp. 20140680 ◽  
Author(s):  
Stineke van Houte ◽  
Monique M. van Oers ◽  
Yue Han ◽  
Just M. Vlak ◽  
Vera I. D. Ros
Keyword(s):  
Spodoptera Exigua ◽  
Behavioural Change ◽  
Parasite Transmission ◽  
Host Manipulation ◽  
Light Perception ◽  
Phototactic Response ◽  
Baculovirus Infection ◽  
Climbing Behaviour ◽  
Host Behaviour ◽  
Underlying Processes

Many parasites manipulate host behaviour to enhance parasite transmission and survival. A fascinating example is baculoviruses, which often induce death in caterpillar hosts at elevated positions (‘tree-top’ disease). To date, little is known about the underlying processes leading to this adaptive host manipulation. Here, we show that the baculovirus Spodoptera exigua multiple nucleopolyhedrovirus (SeMNPV) triggers a positive phototactic response in S. exigua larvae prior to death and causes the caterpillars to die at elevated positions. This light-dependent climbing behaviour is specific for infected larvae, as movement of uninfected caterpillars during larval development was light-independent. We hypothesize that upon infection, SeMNPV captures a host pathway involved in phototaxis and/or light perception to induce this remarkable behavioural change.

scholarly journals Bacmid Expression of Granulovirus Enhancin En3 Accumulates in Cell Soluble Fraction to Potentiate Nucleopolyhedrovirus Infection

Viruses ◽  
2021 ◽  
Vol 13 (7) ◽  
pp. 1233
Author(s):  
Adriana Ricarte-Bermejo ◽  
Oihane Simón ◽  
Ana Beatriz Fernández ◽  
Trevor Williams ◽  
Primitivo Caballero
Keyword(s):  
Trichoplusia Ni ◽  
Recombinant Virus ◽  
Spodoptera Exigua ◽  
Insect Cells ◽  
Soluble Fraction ◽  
Autographa Californica ◽  
Insect Midgut ◽  
Baculovirus Infection ◽  
Occlusion Bodies ◽  
Infected Cells

Enhancins are metalloproteinases that facilitate baculovirus infection in the insect midgut. They are more prevalent in granuloviruses (GVs), constituting up to 5% of the proteins of viral occlusion bodies (OBs). In nucleopolyhedroviruses (NPVs), in contrast, they are present in the envelope of the occlusion-derived virions (ODV). In the present study, we constructed a recombinant Autographa californica NPV (AcMNPV) that expressed the Trichoplusia ni GV (TnGV) enhancin 3 (En3), with the aim of increasing the presence of enhancin in the OBs or ODVs. En3 was successfully produced but did not localize to the OBs or the ODVs and accumulated in the soluble fraction of infected cells. As a result, increased OB pathogenicity was observed when OBs were administered in mixtures with the soluble fraction of infected cells. The mixture of OBs and the soluble fraction of Sf9 cells infected with BacPhEn3 recombinant virus was ~3- and ~4.7-fold more pathogenic than BacPh control OBs in the second and fourth instars of Spodoptera exigua, respectively. In contrast, when purified, recombinant BacPhEn3 OBs were as pathogenic as control BacPh OBs. The expression of En3 in the soluble fraction of insect cells may find applications in the development of virus-based insecticides with increased efficacy.

scholarly journals Homophilic binding of PTP mu, a receptor-type protein tyrosine phosphatase, can mediate cell-cell aggregation

1993 ◽  
Vol 122 (4) ◽  
pp. 961-972 ◽  
Author(s):  
SM Brady-Kalnay ◽  
AJ Flint ◽  
NK Tonks
Keyword(s):  
Fusion Protein ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Recombinant Baculovirus ◽  
Sf9 Cells ◽  
Homophilic Binding ◽  
Protein Tyrosine ◽  
Baculovirus Infection ◽  
Induced Aggregation ◽  
Cell Cell

The receptor-like protein tyrosine phosphatase, PTPmu, displays structural similarity to cell-cell adhesion molecules of the immunoglobulin superfamily. We have investigated the ability of human PTPmu to function in such a capacity. Expression of PTPmu, with or without the PTPase domains, by recombinant baculovirus infection of Sf9 cells induced their aggregation. However, neither a chimeric form of PTPmu, containing the extracellular and transmembrane segments of the EGF receptor and the intracellular segment of PTPmu, nor the intracellular segment of PTPmu expressed as a soluble protein induced aggregation. PTPmu mediates aggregation via a homophilic mechanism, as judged by lack of incorporation of uninfected Sf9 cells into aggregates of PTPmu-expressing cells. Homophilic binding has been demonstrated between PTPmu-coated fluorescent beads (Covaspheres) and endogenously expressed PTPmu on MvLu cells. Additionally the PTPmu-coated beads specifically bound to a bacterially expressed glutathione-S-transferase fusion protein containing the extracellular segment of PTPmu (GST/PTPmu) adsorbed to petri dishes. Covaspheres coated with the GST/PTPmu fusion protein aggregated in vitro and also bound to PTPmu expressed endogenously on MvLu cells. These results suggest that the ligand for this transmembrane PTPase is another PTPmu molecule on an adjacent cell. Thus homophilic binding interactions may be an important component of the function of PTPmu in vivo.

scholarly journals Studies of the Nucleopolyhedrovirus Infection Process in Insects by Using the Green Fluorescence Protein as a Reporter

1998 ◽  
Vol 72 (4) ◽  
pp. 3377-3382 ◽  
Author(s):  
John W. Barrett ◽  
Andy J. Brownwright ◽  
Mark J. Primavera ◽  
Subba Reddy Palli
Keyword(s):  
Fat Body ◽  
Secondary Infection ◽  
Green Fluorescence Protein ◽  
Body Cavity ◽  
Infection Process ◽  
The Body ◽  
Green Fluorescence ◽  
Temporal Regulation ◽  
Baculovirus Infection ◽  
Fluorescence Protein

ABSTRACT A recombinant Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV) expressing the green fluorescence protein (GFP) under the control of the AcMNPV polyhedrin promoter was constructed to study the spatial and temporal regulation of baculovirus infection in a permissive host. Larvae that ingested AcMNPV-GFP showed localized expression of GFP in the midgut epithelial cells, as well as hemocytes, at 24 h postinfection. The presence of fluorescence in these tissues indicated not only that the virus was replicating but also that the very late viral proteins were being synthesized. Secondary infection occurred within the tracheal cells throughout the body cavity, confirming earlier reports, and these foci of infection allowed entry of the virus into other tissues, such as the epidermis and the fat body.

scholarly journals Lipid composition of Spodoptera frugiperda (Sf9) and Trichoplusia ni (Tn) insect cells used for baculovirus infection

FEBS Letters ◽  
1998 ◽  
Vol 441 (1) ◽  
pp. 49-52 ◽  
Author(s):  
Kathrin Marheineke ◽  
Sylvia Grünewald ◽  
William Christie ◽  
Helmut Reiländer
Keyword(s):  
Spodoptera Frugiperda ◽  
Lipid Composition ◽  
Trichoplusia Ni ◽  
Insect Cells ◽  
Baculovirus Infection
Sign in / Sign up

Export Citation Format

Share Document