scholarly journals Lymantria dispar Nucleopolyhedrovirushrf-1 Expands the Larval Host Range of Autographa californica Nucleopolyhedrovirus

1998 ◽  
Vol 72 (3) ◽  
pp. 2526-2531 ◽  
Author(s):  
Chi-Ju Chen ◽  
Martha E. Quentin ◽  
Lynn A. Brennan ◽  
Christine Kukel ◽  
Suzanne M. Thiem
Keyword(s):  
Host Range ◽  
Lymantria Dispar ◽  
Helicoverpa Zea ◽  
Autographa Californica ◽  
Insect Larvae ◽  
Resistant Species ◽  
Larval Host ◽  
Autographa Californica Nucleopolyhedrovirus ◽  
High Doses ◽  
Third Instar Larvae

The gypsy moth (Lymantria dispar) is nonpermissive forAutographa californica nucleopolyhedrovirus (AcNPV) infection. We previously isolated a gene, host range factor 1 (hrf-1), from L. dispar nucleopolyhedrovirus that promotes AcNPV replication in Ld652Y cells, a nonpermissiveL. dispar cell line (S. M. Thiem, X. Du, M. E. Quentin, and M. M. Berner, J. Virol. 70:2221–2229, 1996). In the present study, we investigated the ability of hrf-1 to alter the larval host range of AcNPV. Bioassays using recombinant AcNPV bearing hrf-1 were conducted with insect larvae by use of oral infection. AcNPV bearing hrf-1 was infectious for neonate L. dispar larvae, with a 50% lethal concentration of 1.2 × 105 polyhedral inclusion bodies/ml of diet, which is similar to that of wild-type AcNPV for permissive hosts. AcNPV can kill neonate L. dispar larvae at high doses, but it does not kill third-instar larvae. However, electron microscopy studies of AcNPV-inoculated third-instar larvae revealed virus replication in the midgut cells. PCR analyses indicated that the virus was AcNPV. These results suggest that the block for AcNPV infection of L. dispar larvae is its inability to spread systematically from primary infection sites in the midgut epithelium and that this barrier is leaky in neonates. hrf-1 allows AcNPV to overcome this barrier. AcNPV recombinants bearing hrf-1 were also significantly more infectious for Helicoverpa zea, a resistant species, suggesting that the blocks for AcNPV infection ofL. dispar and H. zea larvae may be similar.

scholarly journals Deletion of the Autographa californica nucleopolyhedrovirus chitinase KDEL motif and in vitro and in vivo analysis of the modified virus

2004 ◽  
Vol 85 (4) ◽  
pp. 821-831 ◽  
Author(s):  
Giles P. Saville ◽  
Alexandra L. Patmanidi ◽  
Robert D. Possee ◽  
Linda A. King
Keyword(s):  
Trichoplusia Ni ◽  
Lethal Dose ◽  
Gene Promoter ◽  
Autographa Californica ◽  
Coding Region ◽  
Insect Larvae ◽  
Autographa Californica Nucleopolyhedrovirus ◽  
Infected Cells

Infection of insect larvae with Autographa californica nucleopolyhedrovirus (AcMNPV) results in the liquefaction of the host, a process involving the action of virus-encoded chitinase and cathepsin gene products. Chitinase is localized in the endoplasmic reticulum (ER) during infection because of the presence of a C-terminal ER retrieval motif (KDEL). In this study, the KDEL coding region was removed from the chitinase gene so that expression of the modified chitinase remained under the control of its own gene promoter, at its native locus. The deletion of KDEL resulted in the redistribution of chitinase within the cell during virus infection. Chitinase lacking the KDEL motif was detectable at the plasma membrane and was also evident in the culture medium of virus-infected cells from as early as 12 h post-infection (p.i.). Secretion of chitinase from the cell continued up to 72 h p.i., until cytolysis. The biological activity of the recombinant virus in Trichoplusia ni larvae was enhanced, with a significant reduction in the lethal dose and lethal time associated with infection. Furthermore, a reduction in feeding damage caused by infected larvae was observed compared to AcMNPV-infected individuals.

Enhancement of Nucleopolyhedrovirus Activity in Helicoverpa zea (Boddie) and Pseudoplusia includens (Walker) Larvae with a Fluorescent Brightener

2001 ◽  
Vol 36 (2) ◽  
pp. 162-168 ◽  
Author(s):  
S. Y. Young
Keyword(s):  
Host Range ◽  
Helicoverpa Zea ◽  
Heliothis Armigera ◽  
Autographa Californica ◽  
The Other ◽  
Pseudoplusia Includens ◽  
Broad Host Range ◽  
Fluorescent Brightener ◽  
Occlusion Bodies ◽  
Anagrapha Falcifera

The enhancement of nucleopolyhedrovirus (NPV) activity by Tinopal® LPW (Tinopal), a stilbene fluorescent brightener, was compared in Helicoverpa zea (Boddie) and Pseudoplusia includens (Walker) using an on-diet bioassay method. Enhancement of the homologous NPV of each species was compared with three heterologous NPV that have a broad host range. In H. zea, the LC50 of H. zea NPV (HzSNPV) alone was 128 occlusion bodies (OBs)/cup, and the LC50 of it and Heliothis armigera NPV (HaMNPV) did not differ significantly. The activity of both viruses improved 18.6 fold when the OB suspension contained 1.0% Tinopal. The LC50s of Autographa californica NPV (AcMNPV) and Anagrapha falcifera NPV (AfMNPV) without Tinopal in H. zea were greater than that of HzSNPV. However, the increase in activity of AcMNPV and AfMNPV at the highest concentrations of Tinopal was two to three fold greater than the increase in activity of HzSNPV. The LC50 of P. includens NPV (PiSNPV) (856 OBs/cup) alone in P. includens was similar to that of AfMNPV and AcMNPV, and much less than that of HaMNPV (19,947 OBs/cup). The addition of Tinopal to the treatment suspension of all four viruses resulted in significantly lower LC50s at all Tinopal concentrations in P. includens. The highest concentration of Tinopal (1.0%) in the OB suspension lowered the LC50 of PiSNPV by 142.7 and AfMNPV by 89.7 fold. Tinopal in the OB suspension lowered the LC50 of AcMNPV and HaMNPV, but they remained less effective than PiSNPV with Tinopal. HaMNPV at all concentrations of Tinopal was much less active in P. includens than the other viruses with or without Tinopal.

scholarly journals Host Range Factor 1 from Lymantria dispar Nucleopolyhedrovirus (NPV) Is an Essential Viral Factor Required for Productive Infection of NPVs in IPLB-Ld652Y Cells Derived from L. dispar

2004 ◽  
Vol 78 (22) ◽  
pp. 12703-12708 ◽  
Author(s):  
Hiroki Ishikawa ◽  
Motoko Ikeda ◽  
Cristiano A. Felipe Alves ◽  
Suzanne M. Thiem ◽  
Michihiro Kobayashi
Keyword(s):  
Host Range ◽  
Lymantria Dispar ◽  
Spodoptera Exigua ◽  
Autographa Californica ◽  
Productive Infection ◽  
Hyphantria Cunea ◽  
Viral Dna ◽  
Global Protein Synthesis ◽  
Viral Factor ◽  
Successful Production

ABSTRACT Host range factor 1 (HRF-1) of Lymantria dispar multinucleocapsid nucleopolyhedrovirus promotes Autographa californica MNPV replication in nonpermissive Ld652Y cells derived from L. dispar. Here we demonstrate that restricted Hyphantria cunea NPV replication in Ld652Y cells was not due to apoptosis but was likely due to global protein synthesis arrest that could be restored by HRF-1. Our data also showed that HRF-1 promoted the production of progeny virions for two other baculoviruses, Bombyx mori NPV and Spodoptera exigua MNPV, whose replication in Ld652Y cells is limited to replication of viral DNA without successful production of infectious progeny virions. Thus, HRF-1 is an essential viral factor required for productive infection of NPVs in Ld652Y cells.

Mutagenesis of the active site coding region of the Autographa californica nucleopolyhedrovirus chiA gene

Microbiology ◽  
2000 ◽  
Vol 81 (5) ◽  
pp. 1403-1411 ◽  
Author(s):  
Carole J. Thomas ◽  
Graham W. Gooday ◽  
Linda A. King ◽  
Robert D. Possee
Keyword(s):  
Active Site ◽  
Trichoplusia Ni ◽  
Active Sites ◽  
Autographa Californica ◽  
Coding Region ◽  
Insect Larvae ◽  
Recombinant Viruses ◽  
Autographa Californica Nucleopolyhedrovirus ◽  
Infected Insect ◽  
Aspartate Residue

The chitinase of Autographa californica nucleopolyhedrovirus (AcMNPV) is required for the characteristic liquefaction of baculovirus-infected insect larvae. Alignments of the putative active sites of a range of chitinases revealed two highly conserved residues, glutamate and aspartate, which have been proposed to constitute the catalytic residues of the active site. These residues were mutated in the AcMNPV chitinase. Three recombinant viruses were generated, AcchiA D311G, AcchiA E315G and AcchiA D311G E315G, which contained mutations at either the glutamate, the aspartate or both. It was demonstrated that chitinase protein production was unaffected by the mutation of these residues. However, mutation of both residues resulted in the attenuation of chitinolytic activity and the cessation of liquefaction of Trichoplusia ni larvae infected with AcchiA D311G E315G. Mutagenesis of the glutamate residue led to a reduction in exochitinase activity and a delay in the appearance of endochitinase activity. In addition, larvae infected with this virus, AcchiA E315G, liquefied more slowly than those larvae infected with wild-type AcMNPV. Mutagenesis of the aspartate residue resulted in a reduction of exochitinase activity but an unexpected enhancement of endochitinolytic activity. Liquefaction of AcchiA D311G-infected larvae was observed at the same time as that of AcMNPV-infected larvae.

scholarly journals In vitro host range of Autographa californica nucleopolyhedrovirus recombinants lacking functional p35, iap1 or iap2.

1999 ◽  
Vol 80 (4) ◽  
pp. 1055-1066 ◽  
Author(s):  
C M Griffiths ◽  
A L Barnett ◽  
M D Ayres ◽  
J Windass ◽  
L A King ◽  
...  
Keyword(s):  
Host Range ◽  
Autographa Californica ◽  
Autographa Californica Nucleopolyhedrovirus

scholarly journals A Functional F Analogue of Autographa californica Nucleopolyhedrovirus GP64 from the Agrotis segetum Granulovirus

2008 ◽  
Vol 82 (17) ◽  
pp. 8922-8926 ◽  
Author(s):  
Feifei Yin ◽  
Manli Wang ◽  
Ying Tan ◽  
Fei Deng ◽  
Just M. Vlak ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Plutella Xylostella ◽  
Syncytium Formation ◽  
Low Ph ◽  
Autographa Californica ◽  
Agrotis Segetum ◽  
Induced Membrane ◽  
F Protein ◽  
Autographa Californica Nucleopolyhedrovirus

ABSTRACT The envelope fusion protein F of Plutella xylostella granulovirus is a computational analogue of the GP64 envelope fusion protein of Autographa californica nucleopolyhedrovirus (AcMNPV). Granulovirus (GV) F proteins were thought to be unable to functionally replace GP64 in the AcMNPV pseudotyping system. In the present study the F protein of Agrotis segetum GV (AgseGV) was identified experimentally as the first functional GP64 analogue from GVs. AgseF can rescue virion propagation and infectivity of gp64-null AcMNPV. The AgseF-pseudotyped AcMNPV also induced syncytium formation as a consequence of low-pH-induced membrane fusion.

scholarly journals Autographa californica Nucleopolyhedrovirus AC141 (Exon0), a Potential E3 Ubiquitin Ligase, Interacts with Viral Ubiquitin and AC66 To Facilitate Nucleocapsid Egress

2017 ◽  
Vol 92 (3) ◽  
Author(s):  
Siddhartha Biswas ◽  
Leslie G. Willis ◽  
Minggang Fang ◽  
Yingchao Nie ◽  
David A. Theilmann
Keyword(s):  
Ubiquitin Ligase ◽  
Nuclear Export ◽  
Molecular Mechanisms ◽  
Nuclear Periphery ◽  
E3 Ubiquitin Ligase ◽  
Autographa Californica ◽  
Nucleocapsid Proteins ◽  
Systemic Spread ◽  
Autographa Californica Nucleopolyhedrovirus ◽  
Budded Virus

ABSTRACTDuring the infection cycle of Autographa californica multiple nucleopolyhedrovirus (AcMNPV), two forms of virions are produced, budded virus (BV) and occlusion-derived virus (ODV). Nucleocapsids that form BV have to egress from the nucleus, whereas nucleocapsids that form ODV remain inside the nucleus. The molecular mechanism that determines whether nucleocapsids remain inside or egress from the nucleus is unknown. AC141 (a predicted E3 ubiquitin ligase) and viral ubiquitin (vUbi) have both been shown to be required for efficient BV production. In this study, it was hypothesized that vUbi interacts with AC141, and in addition, that this interaction was required for BV production. Deletion of bothac141andvubirestricted viral infection to a single cell, and BV production was completely eliminated. AC141 was ubiquitinated by either vUbi or cellular Ubi, and this interaction was required for optimal BV production. Nucleocapsids in BV, but not ODV, were shown to be specifically ubiquitinated by vUbi, including a 100-kDa protein, as well as high-molecular-weight conjugates. The viral ubiquitinated 100-kDa BV-specific nucleocapsid protein was identified as AC66, which is known to be required for BV production and was shown by coimmunoprecipitation and mass spectrometry to interact with AC141. Confocal microscopy also showed that AC141, AC66, and vUbi interact at the nuclear periphery. These results suggest that ubiquitination of nucleocapsid proteins by vUbi functions as a signal to determine if a nucleocapsid will egress from the nucleus and form BV or remain in the nucleus to form ODV.IMPORTANCEBaculoviruses produce two types of virions called occlusion-derived virus (ODV) and budded virus (BV). ODVs are required for oral infection, whereas BV enables the systemic spread of virus to all host tissues, which is critical for killing insects. One of the important steps for BV production is the export of nucleocapsids out of the nucleus. This study investigated the molecular mechanisms that enable the selection of nucleocapsids for nuclear export instead of being retained within the nucleus, where they would become ODV. Our data show that ubiquitination, a universal cellular process, specifically tags nucleocapsids of BV, but not those found in ODV, using a virus-encoded ubiquitin (vUbi). Therefore, ubiquitination may be the molecular signal that determines if a nucleocapsid is destined to form a BV, thus ensuring lethal infection of the host.

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