scholarly journals Sequence and organization of the Spodoptera exigua multicapsid nucleopolyhedrovirus genome

1999 ◽  
Vol 80 (12) ◽  
pp. 3289-3304 ◽  
Author(s):  
Wilfred F. J. IJkel ◽  
Elisabeth A. van Strien ◽  
Jacobus G. M. Heldens ◽  
René Broer ◽  
Douwe Zuidema ◽  
...  
Keyword(s):  
Spodoptera Exigua ◽  
Autographa Californica ◽  
Recent Common Ancestor ◽  
Computer Assisted ◽  
Glycoprotein Gene ◽  
Orgyia Pseudotsugata ◽  
Group I ◽  
Group Ii ◽  
Budded Virus ◽  
Assisted Analysis

The nucleotide sequence of the DNA genome of Spodoptera exigua multicapsid nucleopolyhedrovirus (SeMNPV), a group II NPV, was determined and analysed. The genome contains 135611 bp and has a G+C content of 44 mol%. Computer-assisted analysis revealed 139 ORFs of 150 nucleotides or larger; 103 have homologues in Autographa californica MNPV (AcMNPV) and a further 16 have homologues in other baculoviruses. Twenty ORFs are unique to SeMNPV. Major differences in SeMNPV gene content and arrangement were found compared with the group I NPVs AcMNPV, Bombyx mori (Bm) NPV and Orgyia pseudotsugata (Op) MNPV and the group II NPV Lymantria dispar (Ld) MNPV. Eighty-five ORFs were conserved among all five baculoviruses and are considered as candidate core baculovirus genes. Two putative p26 and odv-e66 homologues were identified in SeMNPV, each of which appeared to have been acquired independently and not by gene duplication. The SeMNPV genome lacks homologues of the major budded virus glycoprotein gene gp64, the immediate-early transactivator ie-2 and bro (baculovirus repeat ORF) genes that are found in AcMNPV, BmNPV, OpMNPV and LdMNPV. Gene parity analysis of baculovirus genomes suggests that SeMNPV and LdMNPV have a recent common ancestor and that they are more distantly related to the group I baculoviruses AcMNPV, BmNPV and OpMNPV. The orientation of the SeMNPV genome is reversed compared with the genomes of AcMNPV, BmNPV, OpMNPV and LdMNPV. However, the gene order in the ‘central’ part of baculovirus genomes is highly conserved and appears to be a key feature in the alignment of baculovirus genomes.

scholarly journals The sequence of the Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus genome

2001 ◽  
Vol 82 (1) ◽  
pp. 241-257 ◽  
Author(s):  
Xinwen Chen ◽  
Wilfred F. J. IJkel ◽  
Renato Tarchini ◽  
Xiulian Sun ◽  
Hans Sandbrink ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Amino Acid Identity ◽  
Computer Assisted ◽  
Structural Genomic ◽  
Orgyia Pseudotsugata ◽  
Group I ◽  
Helicoverpa Armígera ◽  
Group Ii ◽  
Budded Virus ◽  
Assisted Analysis

The nucleotide sequence of the Helicoverpa armigera single-nucleocapsid nucleopolyhedrovirus (HaSNPV) DNA genome was determined and analysed. The circular genome encompasses 131403 bp, has a G+C content of 39·1 mol% and contains five homologous regions with a unique pattern of repeats. Computer-assisted analysis revealed 135 putative ORFs of 150 nt or larger; 100 ORFs have homologues in Autographa californica multicapsid NPV (AcMNPV) and a further 15 ORFs have homologues in other baculoviruses such as Lymantria dispar MNPV (LdMNPV), Spodoptera exigua MNPV (SeMNPV) and Xestia c-nigrum granulovirus (XcGV). Twenty ORFs are unique to HaSNPV without homologues in GenBank. Among the six previously sequenced baculoviruses, AcMNPV, Bombyx mori NPV (BmNPV), Orgyia pseudotsugata MNPV (OpMNPV), SeMNPV, LdMNPV and XcGV, 65 ORFs are conserved and hence are considered as core baculovirus genes. The mean overall amino acid identity of HaSNPV ORFs was the highest with SeMNPV and LdMNPV homologues. Other than three ‘baculovirus repeat ORFs’ (bro) and two ‘inhibitor of apoptosis’ (iap) genes, no duplicated ORFs were found. A putative ORF showing similarity to poly(ADP-ribose) glycohydrolases (parg) was newly identified. The HaSNPV genome lacks a homologue of the major budded virus (BV) glycoprotein gene, gp64, of AcMNPV, BmNPV and OpMNPV. Instead, a homologue of SeMNPV ORF8, encoding the major BV envelope protein, has been identified. GeneParityPlot analysis suggests that HaSNPV, SeMNPV and LdMNPV (group II) have structural genomic features in common and are distinct from the group I NPVs and from the granuloviruses. Cluster alignment between group I and group II baculoviruses suggests that they have a common ancestor.

scholarly journals The F-Like Protein Ac23 Enhances the Infectivity of the Budded Virus of gp64-Null Autographa californica Multinucleocapsid Nucleopolyhedrovirus Pseudotyped with Baculovirus Envelope Fusion Protein F

2008 ◽  
Vol 82 (19) ◽  
pp. 9800-9804 ◽  
Author(s):  
Manli Wang ◽  
Ying Tan ◽  
Feifei Yin ◽  
Fei Deng ◽  
Just M. Vlak ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Fusion Proteins ◽  
Spodoptera Exigua ◽  
Autographa Californica ◽  
Pseudotyped Virus ◽  
F Protein ◽  
Group I ◽  
Protein F ◽  
Budded Virus ◽  
Functional Envelope

ABSTRACT The GP64 and F proteins were previously identified as the sole functional envelope fusion proteins in Baculoviridae. F-like proteins, present only in group I nucleopolyhedroviruses (NPVs), are remnant, nonfunctional F proteins. In this report, we describe the effect of the presence or absence of the F-like protein Ac23 in a gp64-null Autographa californica multinucleocapsid NPV pseudotyped with the F protein from Spodoptera exigua multicapsid NPV (SeF). We found that the presence of Ac23 elevates the infectivity of the pseudotyped virus. This is in contrast to the results of Lung et al. (J. Virol. 76:5729-5736, 2002), who found no such effect. The possible reasons for the differing results are discussed.

scholarly journals GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses

2008 ◽  
Vol 89 (2) ◽  
pp. 424-431 ◽  
Author(s):  
Marcel Westenberg ◽  
Just M. Vlak
Keyword(s):  
Fusion Protein ◽  
Selective Advantage ◽  
Autographa Californica ◽  
Viral Attachment ◽  
F Protein ◽  
Group I ◽  
The Family ◽  
Protein Group ◽  
Group Ii ◽  
Budded Virus

The genus Nucleopolyhedrovirus (NPV) of the family Baculoviridae can be subdivided phylogenetically into two groups. The same division can be made on the basis of their budded virus (BV) envelope fusion protein. Group I NPVs are characterized by the presence of a GP64-like major envelope fusion protein, which is involved in viral attachment and the fusion of virus and cell membrane, and is required for budding of progeny nucleocapsids. Group II NPVs have an envelope fusion protein unrelated to GP64, named F. In contrast to GP64, F proteins are found in all baculoviruses, but they are not functional as envelope fusion proteins in group I NPVs. Autographa californica multiple NPV (AcMNPV) lacking GP64 can be pseudotyped by the F protein of Spodoptera exigua multiple NPV (SeMNPV), suggesting that F proteins are functionally analogous to GP64. GP64 homologues are thought to have been acquired by group I NPVs during evolution, thereby giving these viruses a selective advantage and obviating the need for a functional F protein. To address this supposition experimentally, attempts were made to pseudotype a group II NPV, SeMNPV, with GP64. Transfection of an f-null SeMNPV bacmid into Se301 cells did not result in the production of infectious BVs. This defect was rescued by insertion of SeMNPV f, but not by insertion of AcMNPV gp64. This suggests that the functional analogy between GP64 and F is not readily reciprocal and that F proteins from group II NPVs may provide additional functions in BV formation that are lacking in the GP64 type of fusion protein.

Efficacy of Computer-Assisted Management of Respiratory Failure in Neonates

PEDIATRICS ◽  
1986 ◽  
Vol 78 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Waldemar A. Carlo ◽  
Lucia Pacifico ◽  
Robert L. Chatburn ◽  
Avroy A. Fanaroff
Keyword(s):  
Respiratory Failure ◽  
Computer Program ◽  
Computer Assisted ◽  
Blood Gas ◽  
Arterial Blood Gas ◽  
Group Iii ◽  
Arterial Blood ◽  
Group I ◽  
Group Ii ◽  
Assisted Management

We modified an algorithm for mechanical ventilation of infants with respiratory distress syndrome to create an interactive user-friendly computer program. To determine the effectiveness of this computer program, we evaluated the correction of deranged arterial blood gases in three groups of neonates: group I, treated before the introduction of the computer into the nursery; group II, managed by pediatric residents with the guidance of the computer program; group III, treated after the introduction of the computer into the nursery but managed without consideration of the computer output. Arterial blood gas values improved more frequently in the neonates managed with computer consultation (group II, 65/75, 87%) than in both control groups (group I, 37/57, 65%, P < .005; and group III, 46/63, 73%, P < .05). Furthermore, increases in ventilatory support in the presence of normal arterial blood gas values occurred only in patients managed without computer guidance. In a teaching institution, more effective care of neonates with respiratory failure may be facilitated by computer-assisted management of mechanical ventilators.

scholarly journals The F protein of Helicoverpa armigera single nucleopolyhedrovirus can be substituted functionally with its homologue from Spodoptera exigua multiple nucleopolyhedrovirus

2008 ◽  
Vol 89 (3) ◽  
pp. 791-798 ◽  
Author(s):  
Manli Wang ◽  
Ying Tan ◽  
Feifei Yin ◽  
Fei Deng ◽  
Just M. Vlak ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Spodoptera Exigua ◽  
Late Phase ◽  
Positive Control ◽  
Host Proteins ◽  
F Protein ◽  
Helicoverpa Armígera ◽  
Group Ii ◽  
Budded Virus ◽  
Species Specific

F proteins of group II nucleopolyhedroviruses (NPVs) are envelope fusion proteins essential for virus entry and egress. An F-null Helicoverpa armigera single nucleocapsid NPV (HearNPV) bacmid, HaBacΔF, was constructed. This bacmid could not produce infectious budded virus (BV) when transfected into HzAM1 cells, showing that F protein is essential for cell-to-cell transmission of BVs. When HaBacΔF was pseudotyped with the homologous F protein (HaBacΔF-HaF, positive control) or with the heterologous F protein from Spodoptera exigua multinucleocapsid NPV (SeMNPV) (HaBacΔF-SeF), infectious BVs were produced with similar kinetics. In the late phase of infection, the BV titre of HaBacΔF-SeF virus was about ten times lower than that of HaBacΔF-HaF virus. Both pseudotyped viruses were able to fuse HzAM1 cells in a similar fashion. The F proteins of both HearNPV and SeMNPV were completely cleaved into F1 and F2 in the BVs of vHaBacΔF-HaF and vHaBacΔF-SeF, respectively, but the cleavage of SeF in vHaBacΔF-SeF-infected HzAM1 cells was incomplete, explaining the lower BV titre of vHaBacΔF-SeF. Polyclonal antisera against HaF1 and SeF1 specifically neutralized the infection of vHaBacΔF-HaF and vHaBacΔF-SeF, respectively. HaF1 antiserum showed some cross-neutralization with vHaBacΔF-SeF. These results demonstrate that group II NPV F proteins can be functionally replaced with a homologue of other group II NPVs, suggesting that the interaction of F with other viral or host proteins is not absolutely species-specific.

scholarly journals The complete sequence of the Cydia pomonella granulovirus genome

2001 ◽  
Vol 82 (10) ◽  
pp. 2531-2547 ◽  
Author(s):  
Teresa Luque ◽  
Ruth Finch ◽  
Norman Crook ◽  
David R. O’Reilly ◽  
Doreen Winstanley
Keyword(s):  
Cydia Pomonella ◽  
Protein Tyrosine Phosphatases ◽  
Complete Sequence ◽  
Autographa Californica ◽  
Glycoprotein Gene ◽  
Repeat Sequences ◽  
Budded Virus ◽  
Cydia Pomonella Granulovirus ◽  
High Level ◽  
Imperfect Palindrome

The nucleotide sequence of the DNA genome of Cydia pomonella granulovirus (CpGV) was determined and analysed. The genome is composed of 123500 bp and has a G+C content of 45·2%. It contains 143 ORFs of 150 nucleotides or more that show minimal overlap. One-hundred-and-eighteen (82·5%) of these putative genes are homologous to genes previously identified in other baculoviruses. Among them, 73 are homologous to genes of Autographa californica nucleopolyhedrovirus (AcMNPV), whereas 108 and 98 are homologous to genes of Xestia c-nigrum GV (XcGV) and Plutella xylostella GV (PxGV), respectively. These homologues show on average 37·4% overall amino acid sequence identity to those from AcMNPV and 45% to those from XcGV and PxGV. The CpGV gene content was compared to that of other baculoviruses. Several genes reported to have major roles in baculovirus biology were not found in the CpGV genome, such as gp64, the major budded virus glycoprotein gene in some nucleopolyhedroviruses, and lef-7, involved in DNA replication. However, the CpGV genome encodes the large and small subunits of ribonucleotide reductase, three inhibitor of apoptosis (iap) homologues and two protein tyrosine phosphatases. The CpGV, PxGV and XcGV genomes present a noticeably high level of conservation of gene order and orientation. A striking feature of the CpGV genome is the absence of typical homologous repeat sequences. However, it contains one major repeat region and 13 copies of a single 73–77 bp imperfect palindrome.

scholarly journals Treatment of pediatric patients with lower leg deformities associated with physeal arrest: analysis of 28 cases

2017 ◽  
Vol 5 (4) ◽  
pp. 38-47
Author(s):  
Viktor A. Vilensky ◽  
Andrey A. Pozdeev ◽  
Timur F. Zubairov ◽  
Ekaterina A. Zakharyan
Keyword(s):  
External Fixation ◽  
Growth Plate ◽  
Deformity Correction ◽  
Limb Length Discrepancy ◽  
Lower Leg ◽  
Computer Assisted ◽  
Mechanical Axis Deviation ◽  
Group I ◽  
Group Ii ◽  
Healthy Part

Aim. To retrospectively analyze the results of two treatment methods for lower leg deformities associated with partial growth arrest. Materials and methods. Group I comprised 15 children who underwent osteotomy, acute overcorrection, and external fixation by Ilizarov with subsequent lengthening of the segment. Group II comprised 13 patients who underwent epiphysiodesis of the healthy part of the growth plate by drilling, osteotomy with external fixation by use of an Ortho-SUV Frame, and subsequent gradual deformity correction and lengthening. Results. In group I, overcorrection of varus deformities by mechanical axis deviation (MAD) was 18.28 ± 5.25 mm, overcorrection by mechanical medial proximal tibial angle (mMPTA) was 14.86 ± 4.45°, and overcorrection by mechanical lateral distal tibial angle (mLDTA) was 12.85 ± 3.02°. Overcorrection of valgus deformities according to MAD was 15.12 ± 8.28 mm, overcorrection by mMPTA was 10.38 ± 2.77°, and overcorrection by mLDTA was 7.5 ± 3.9°. Recurrence of the deformity was observed in 11 (73%) cases (range, 5–16 months). In group II, the accuracy of correction (AC) in varus deformities for MAD was 98% and 94% for mMPTA and mLDTA. For valgus deformities, AC for MAD was 90% and 96% for mMPTA and mLDTA. The AC for anatomical proximal posterior tibial angle and anatomical anterior distal tibial angle was 96% for procurvation deformities and that for recurvation deformities was 92%. Deformity recurrence was observed in only one case within 6 months after frame removal. In 2 cases, repeat limb length discrepancy correction surgeries were performed. Conclusion. Use of epiphysiodesis of the healthy portion of the growth plate in combination with osteotomy, computer-assisted external fixation with subsequent gradual deformity correction, and lengthening in patients with deformities associated with partial physeal arrest significantly decreased the number of deformity recurrences.

Low density lipoprotein on poor quality mithun (Bos frontalis) semen preservation

2016 ◽  
Author(s):  
P. Perumal ◽  
S. K. Srivastava ◽  
K. K. Baruah ◽  
J. S. Rajoriya ◽  
N. Srivastava
Keyword(s):  
Density Lipoprotein ◽  
Egg Yolk ◽  
Cholesterol Content ◽  
Poor Quality ◽  
Computer Assisted ◽  
Low Density ◽  
Liquid Storage ◽  
Group I ◽  
Intracellular Enzymes ◽  
Group Ii

Low density lipoproteins (LDL) extracted from hens egg yolk (EY) has been studied over EY based extender for liquid storage of mithun semen with the objective to explore the use of LDL in place of EY. Physio-morphological attributes (PMAs) and mobility and velocity parameters were measured by computer assisted sperm analyser (CASA). Leakage of intracellular enzymes, activity of total antioxidants and lipid peroxidation following liquid storage (5oC) of mithun semen were studied. Fifty ejaculates were collected through transrectal massage method from matured mithun bulls and based on the mass activity and individual motility; the semen samples were splited into good and poor quality and diluted with the tris citrate glycerol (TCG) extender and were splited into three equal aliquots: Group I: Control, EY; Group II and Group III contained 8 and 10% LDL (w/v), respectively. PMAs, intracellular enzymatic leakage and biochemical profiles were evaluated at 5°C following 10hrs incubation. Result revealed a significant (p less than 0.05) improvement in PMAs, CASA parameters and cholesterol content of spermatozoa as well as reduction in leakage of intracellular enzymes, oxidative stress in Group II than control and other treatment group. It was concluded that addition of 8% LDL holds a clear advantage over EY or 10% LDL in liquid preservation of mithun semen.

scholarly journals Induction of apoptosis in an insect cell line, IPLB-Ld652Y, infected with nucleopolyhedroviruses

2003 ◽  
Vol 84 (3) ◽  
pp. 705-714 ◽  
Author(s):  
Hiroki Ishikawa ◽  
Motoko Ikeda ◽  
Kenichi Yanagimoto ◽  
Cristiano A. Felipe Alves ◽  
Yasuhiro Katou ◽  
...  
Keyword(s):  
Caspase 3 ◽  
Spodoptera Exigua ◽  
Insect Cell Line ◽  
High Titre ◽  
Autographa Californica ◽  
Apoptotic Response ◽  
Hyphantria Cunea ◽  
Orgyia Pseudotsugata ◽  
Virion Production ◽  
Induced Apoptosis

Ld652Y cells derived from the gypsy moth, Lymantria dispar, were infected with seven different nucleopolyhedroviruses (NPVs) including those from Autographa californica, Bombyx mori (BmNPV), Hyphantria cunea (HycuNPV), Spodoptera exigua (SeMNPV), L. dispar, Orgyia pseudotsugata (OpMNPV) and Spodoptera litura (SpltMNPV). The results showed that Ld652Y cells infected with BmNPV, HycuNPV, SeMNPV, OpMNPV and SpltMNPV underwent apoptosis, displaying apoptotic bodies, characteristic DNA fragmentation and increased caspase-3-like protease activity; HycuNPV induced the most severe apoptosis. In HycuNPV-infected Ld652Y cells, a considerable amount of viral DNA was synthesized although there was no detectable yield of budded virions and polyhedrin. Northern blot and immunoblot analyses revealed that HycuNPV inhibitor of apoptosis 3 (IAP3), which has been shown to function in Sf9 cells, was expressed in HycuNPV-infected Ld652Y cells at a level higher than or comparable with that in HycuNPV-infected SpIm cells, which produced a high titre of progeny virions without any apoptotic response. These results imply that the relative ease of apoptosis induction in NPV-infected Ld652Y cells is largely dependent on inherent cellular properties rather than functions of the respective NPVs, and indicate that the defect in progeny virion production is not merely due to the virus-induced apoptosis in HycuNPV-infected Ld652Y cells.

scholarly journals Ac23, an Envelope Fusion Protein Homolog in the Baculovirus Autographa californica Multicapsid Nucleopolyhedrovirus, Is a Viral Pathogenicity Factor

2003 ◽  
Vol 77 (1) ◽  
pp. 328-339 ◽  
Author(s):  
Oliver Y. Lung ◽  
Marilyn Cruz-Alvarez ◽  
Gary W. Blissard
Keyword(s):  
Fusion Protein ◽  
Viral Entry ◽  
Fusion Proteins ◽  
Autographa Californica ◽  
Viral Envelope ◽  
Evolutionary Divergence ◽  
Pathogenicity Factor ◽  
Group I ◽  
Group Ii ◽  
Contrast Group

ABSTRACT Viral envelope fusion proteins are important structural proteins that mediate viral entry and may affect or determine the host range of a virus. The acquisition, exchange, and evolution of such envelope proteins may dramatically affect the success and evolutionary divergence of viruses. In the family Baculoviridae, two very different envelope fusion proteins have been identified. Budded virions of group I nucleopolyhedroviruses (NPVs) such as the Autographa californica multicapsid nucleopolyhedrovirus (AcMNPV), contain the essential GP64 envelope fusion protein. In contrast group II NPVs and granuloviruses have no gp64 gene but instead encode a different envelope protein called F. F proteins from group II NPVs can functionally substitute for GP64 in gp64null AcMNPV viruses, indicating that GP64 and these F proteins serve a similar functional role. Interestingly, AcMNPV (and other gp64-containing group I NPVs) also contain an F gene homolog (Ac23) but the AcMNPV F homolog cannot compensate for the loss of gp64. In the present study, we show that Ac23 is expressed and is found in budded virions. To examine the function of F protein homologs from the gp64-containing baculoviruses, we generated an Ac23null AcMNPV genome by homologous recombination in E. coli. We found that Ac23 was not required for viral replication or pathogenesis in cell culture or infected animals. However, Ac23 accelerated the mortality of infected insect hosts by approximately 28% or 26 h. Thus, Ac23 represents an important viral pathogenicity factor in larvae infected with AcMNPV.

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