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 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 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 Proteomics Analysis of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Identified Two New Occlusion-Derived Virus-Associated Proteins, HA44 and HA100

2007 ◽  
Vol 81 (17) ◽  
pp. 9377-9385 ◽  
Author(s):  
Fei Deng ◽  
Ranran Wang ◽  
Minggang Fang ◽  
Yue Jiang ◽  
Xushi Xu ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Structural Proteins ◽  
Proteomics Analysis ◽  
Group I ◽  
Associated Proteins ◽  
Helicoverpa Armígera ◽  
Group Ii ◽  
First Time

ABSTRACT Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometry were used to analyze the structural proteins of the occlusion-derived virus (ODV) of Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV), a group II NPV. Twenty-three structural proteins of HearNPV ODV were identified, 21 of which have been reported previously as structural proteins or ODV-associated proteins in other baculoviruses. These include polyhedrin, P78/83, P49, ODV-E18, ODV-EC27, ODV-E56, P74, LEF-3, HA66 (AC66), DNA polymerase, GP41, VP39, P33, ODV-E25, helicase, P6.9, ODV/BV-C42, VP80, ODV-EC43, ODV-E66, and PIF-1. Two proteins encoded by HearNPV ORF44 (ha44) and ORF100 (ha100) were discovered as ODV-associated proteins for the first time. ha44 encodes a protein of 378 aa with a predicted mass of 42.8 kDa. ha100 encodes a protein of 510 aa with a predicted mass of 58.1 kDa and is a homologue of the gene for poly(ADP-ribose) glycohydrolase (parg). Western blot analysis and immunoelectron microscopy confirmed that HA44 is associated with the nucleocapsid and HA100 is associated with both the nucleocapsid and the envelope of HearNPV ODV. HA44 is conserved in group II NPVs and granuloviruses but does not exist in group I NPVs, while HA100 is conserved only in group II NPVs.

scholarly journals Function, oligomerization and N-linked glycosylation of the Helicoverpa armigera single nucleopolyhedrovirus envelope fusion protein

2006 ◽  
Vol 87 (4) ◽  
pp. 839-846 ◽  
Author(s):  
Gang Long ◽  
Marcel Westenberg ◽  
Hualin Wang ◽  
Just M. Vlak ◽  
Zhihong Hu
Keyword(s):  
Fusion Protein ◽  
Helicoverpa Armigera ◽  
Disulfide Bonds ◽  
Attractive Alternative ◽  
Present Observation ◽  
Reading Frame ◽  
Group I ◽  
The Family ◽  
Helicoverpa Armígera ◽  
Group Ii

In the family Baculoviridae, two distinct envelope fusion proteins are identified in budded virions (BVs). GP64 is the major envelope fusion protein of group I nucleopolyhedrovirus (NPV) BVs. An unrelated type of envelope fusion protein, named F, is encoded by group II NPVs. The genome of Helicoverpa armigera (Hear) NPV, a group II NPV of the single nucleocapsid or S type, also encodes an F-like protein: open reading frame 133 (Ha133). It was demonstrated by N-terminal sequencing of the major 59 kDa protein present in HearNPV BV that this protein is one of the two F subunits: F1 (transmembrane subunit of 59 kDa) and F2 (surface subunit of 20 kDa), both the result of cleavage by a proprotein convertase and disulfide-linked. The HearNPV F protein proved to be a functional analogue of GP64, as the infectivity of an AcMNPV gp64-deletion mutant was rescued by the introduction of the HearNPV F gene. It was also demonstrated by chemical cross-linking that HearNPV F is present in BVs as an oligomer whereby, unlike GP64, disulfide bonds are not involved. Deglycosylation assays indicated that both F1 and F2 possess N-linked glycans. However, when F was made in Hz2E5 cells, these glycans did not have an α-1-3 core fucose modification that usually occurs in insect cells. As α-1-3 core fucose is a major inducer of an allergic response in humans, the present observation makes the HearNPV–Hz2E5 system an attractive alternative for the production of recombinant glycoproteins for therapeutic use in humans.

scholarly journals Partial Functional Rescue of Helicoverpa armigera Single Nucleocapsid Nucleopolyhedrovirus Infectivity by Replacement of F Protein with GP64 from Autographa californica Multicapsid Nucleopolyhedrovirus

2010 ◽  
Vol 84 (21) ◽  
pp. 11505-11514 ◽  
Author(s):  
Manli Wang ◽  
Feifei Yin ◽  
Shu Shen ◽  
Ying Tan ◽  
Fei Deng ◽  
...  
Keyword(s):  
Helicoverpa Armigera ◽  
Culture Supernatant ◽  
Selective Advantage ◽  
Autographa Californica ◽  
Cell Culture Supernatant ◽  
F Protein ◽  
Group I ◽  
Control Virus ◽  
Helicoverpa Armígera ◽  
Group Ii

ABSTRACT Two distinct envelope fusion proteins (EFPs) (GP64 and F) have been identified in members of the Baculoviridae family of viruses. F proteins are found in group II nucleopolyhedroviruses (NPVs) of alphabaculoviruses and in beta- and deltabaculoviruses, while GP64 occurs only in group I NPVs of alphabaculoviruses. It was proposed that an ancestral baculovirus acquired the gp64 gene that conferred a selective advantage and allowed it to evolve into group I NPVs. The F protein is a functional analogue of GP64, as evidenced from the rescue of gp64-null Autographa californica multicapsid nucleopolyhedrovirus (MNPV) (AcMNPV) by F proteins from group II NPVs or from betabaculoviruses. However, GP64 failed to rescue an F-null Spodoptera exigua MNPV (SeMNPV) (group II NPV). Here, we report the successful generation of an infectious gp64-rescued group II NPV of Helicoverpa armigera (vHaBacΔF-gp64). Viral growth curve assays and quantitative real-time PCR (Q-PCR), however, showed substantially decreased infectivity of vHaBacΔF-gp64 compared to the HaF rescue control virus vHaBacΔF-HaF. Electron microscopy further showed that most vHaBacΔF-gp64 budded viruses (BV) in the cell culture supernatant lacked envelope components and contained morphologically aberrant nucleocapsids, suggesting the improper BV envelopment or budding of vHaBacΔF-gp64. Bioassays using pseudotyped viruses with a reintroduced polyhedrin gene showed that GP64-pseudotyped Helicoverpa armigera single nucleocapsid nucleopolyhedrovirus (HearNPV) significantly delayed the mortality of infected H. armigera larvae.

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 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 Gene organization and sequencing of the Choristoneura fumiferana defective nucleopolyhedrovirus genome

2005 ◽  
Vol 86 (4) ◽  
pp. 945-961 ◽  
Author(s):  
Hilary A. M. Lauzon ◽  
Peter B. Jamieson ◽  
Peter J. Krell ◽  
Basil M. Arif
Keyword(s):  
Choristoneura Fumiferana ◽  
Amino Acid Identity ◽  
Gene Organization ◽  
Open Reading Frames ◽  
Anticarsia Gemmatalis ◽  
Orgyia Pseudotsugata ◽  
Eastern Spruce Budworm ◽  
Group I ◽  
Average Amino Acid Identity ◽  
Late Expression

Two distinct nucleopolyhedrovirus species of the eastern spruce budworm, Choristoneura fumiferana, exist in a symbiont-like relationship. C. fumiferana defective nucleopolyhedrovirus (CfDEFNPV) only infects C. fumiferana larvae per os in the presence of C. fumiferana nucleopolyhedrovirus Ireland strain (CfMNPV), but is infective when injected into the haemolymph. CfDEFNPV synergizes CfMNPV in per os infections and CfMNPV is always the predominant progeny. This study was undertaken to report the genomic makeup and organization of CfDEFNPV in an attempt to identify its defect and understand its synergistic role. The genome was mapped, sequenced, characterized and compared to other baculoviruses. The CfDEFNPV genome was 131 160 nt long with 149 putative open reading frames (ORFs) and a G+C content of 45·8 mol%. Homologues of all 62 conserved lepidopteran baculovirus genes were found including those implicated in per os infectivity, p74, per os infectivity factor (pif) and pif-2. Although no obvious deletions were observed to explain the defect, two ORFs, Cfdef79 and Cfdef99 (inhibitor of apoptosis-4), contained potential deletions. Cfdef50 (late expression factor-10)/Cfdef51 (vp1054) and Cfdef76/Cfdef77 (telokin-like protein) had large overlaps and a potential homologue to ac105/he65 was split. Four baculovirus repeat ORFs were present, as were two unique genes, but no enhancins were identified. CfDEFNPV contained 13 homologous regions, each with one to five palindromes. Comparison with fully sequenced baculovirus genomes identified CfDEFNPV as a group I NPV with the closest average amino acid identity to Epiphyas postvittana NPV, followed by Orgyia pseudotsugata MNPV and CfMNPV, with its closest matches being to individual Anticarsia gemmatalis MNPV gene sequences.

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