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PubMed1996

A polymerase chain reaction for the detection of nucleopolyhedroviruses in infected insects: the fate of the Spodoptera littoralis virus in Locusta migratoria.

The Spodoptera littoralis nucleopolyhedrovirus (SlNPV) is a potential pest control agent of Spodoptera spp. As part of our studies to establish the use of this virus, a polymerase chain reaction (PCR)-based method was developed for the detection of viral DNA in infected insects. PCR amplification of the polyhedrin sequences enabled the detection of low levels of viral DNA directly from viral occlusion bodies or from total larval DNA. The use of different sets of synthetic DNA primers allowed us to differentiate between SlNPV and the Autographa californica NPV (AcNPV) and to identify a new AcNPV variant isolated from a cotton pest, Pectinophora gossypiella NPV. The PCR method was also used to test for the possible infection of Locusta migratoria larvae by SlNPV, reported by Bensimon et al., 1987. The progress of SlNPV infection in L. migratoria larvae was monitored by PCR for 2 weeks. The reaction revealed decreasing amounts of viral DNA in infected larvae. During this time, no signs of disease were observed in the infected locusts.

Animals↗
PubMed2005

In vitro biosynthesis of volicitin in Spodoptera litura.

Volicitin [N-(17-hydroxylinolenoyl)-L-glutamine] and N-linolenoyl-L-glutamine, originally identified in the regurgitant of Spodoptera exigua, induce damaged corn leaves to release volatile compounds which enable parasitic wasps to locate host caterpillars. Here we demonstrate the in vitro biosynthesis of volicitin for the first time by using gut tissues of Spodoptera litura larvae, as well as N-linolenoyl-L-glutamine. When crop, midgut tissues, peritrophic membrane and gut contents isolated from S. litura were incubated with sodium linolenate and L-[alpha-15N] glutamine, not only 15N-labeled N-linolenoyl-L-glutamine but 15N-labeled volicitin was detected mainly in the midgut incubation by LCMS and LCMSMS analysis. In contrast, there were negligible amounts of the newly biosynthesized compounds in the gut content incubation. Furthermore, the microsomal fraction obtained from the gut tissues clearly showed specific incorporation of glutamine. This substrate selectivity accounts for the exclusive uptake of glutamine by fatty acid amides (FAAs) in the noctuid caterpillars, even though glutamine was not a major component in the regurgitant. Additionally, intensive chemical analyses revealed that more than 20% of glutamine in hemolymph was present as conjugates in gut contents. These results suggest that FAA compounds are actively synthesized by caterpillar tissues and might play important physiological role(s) in glutamine metabolism.

Animals↗
PubMed2003

A correlation between macronutrient balancing and insect host-plant range: evidence from the specialist caterpillar Spodoptera exempta (Walker).

In an earlier study, we showed that the ingestive responses of the generalist caterpillar Spodoptera littoralis to foods imbalanced in their protein:carbohydrate content is similar to generalist locusts, but differs from that of specialist-feeding locusts. Here we further pursued the comparison by repeating the experiments using a closely related specialist caterpillar, Spodoptera exempta. First, caterpillars were allowed to self-compose a diet of preferred protein:carbohydrate balance by mixing between nutritionally complementary foods. Then, they were confined to one of five imbalanced foods, in which we measured the trade-off between over- and under-ingesting the two nutrients. On complementary foods, the caterpillars actively regulated their protein and carbohydrate intake. In the no-choice experiment, those fed excess-protein foods ingested small surpluses of protein compared with generalist feeders, thus showing a pattern of nutrient balancing similar to that observed in specialist locusts. Utilisation data indicated that ingested excesses and deficits were to some extent offset by differential utilisation. Evidence also showed that post-ingestive responses of the specialist S. exempta were less flexible than those observed in the generalist S. littoralis, a pattern which is again in accordance with comparisons of acridids differing in their host-plant range.

Animals↗
PubMed2006

Spodoptera litura multicapsid nucleopolyhedrovirus inhibits Microplitis bicoloratus polydnavirus-induced host granulocytes apoptosis.

Baculoviruses and parasitoids are critically important biological control agents in integrated pest management (IPM). They have been simultaneously and sequentially used to target insect pests. In this study, we examined the impacts of both baculovirus and polydnavirus (PDV) infection on the host cellular immune response. Larvae of the lepidopteran Spodoptera litura were infected by Spodoptera litura multicapsid nucleopolyhedrovirus (SpltMNPV) and then the animals were parasitized by the braconid wasp Microplitis bicoloratus. The fate of the parasitoids in the dually infected hosts was followed and encapsulation of M. bicoloratus first instar larvae was observed. Hemocytes of S. litura larvae underwent apoptosis in naturally parasitized hosts and in non-parasitized larvae after injection of M. bicoloratus ovarian calyx fluid (containing MbPDV) plus venom (CFPV). However, assessments of the percentages of cells undergoing apoptosis under different treatments indicated that SpltMNPV could inhibit MbPDV-induced apoptosis in hemocytes when hosts were first injected with SpltMNPV budded virus (BV) followed by injection with M. bicoloratus CFPV. As the time of injection with SpltMNPV BV increased, the percentages of apoptosis in hemocytes population declined. Furthermore, in vitro, the percentages of apoptosis showed that SpltMNPV BV could inhibit MbPDV-induced granulocytes apoptosis. The occurrence of MbPDV-induced host granulocytes apoptosis was inhibited in the dually infected hosts. As hemocytes apoptosis causes host immunosuppression, the parasitoids are normally protected from the host immune system. However, in larvae infected with both baculovirus and PDV, the parasitoids underwent encapsulation in the host hemocoel.

Animals↗
PubMed2000

Phosphorylation of the insect immunophilin FKBP46 by the Spodoptera frugiperda homolog of casein kinase II.

Immunophilins are a family of conserved proteins found in both prokaryotes and eukaryotes, that exhibit peptidylprolyl isomerase (PPIase) activity. Members of this family bind to immunosuppressive drugs and on this basis are divided into two classes: FKBPs bind to FK506 and rapamycin, while cyclophilins bind to cyclosporin A. In this paper, we report on insect immunophilin FKBP46 and its associated kinase. The insect FKBP46 belongs to the high-molecular-weight immunophilins and shares many characteristic features with its mammalian counterparts, but its functional role remains unclear. Here, we show that FKBP46 is phosphorylated by a protein kinase present in the nucleus of both insect Spodoptera frugiperda (Sf9) and human Jurkat cells. This protein kinase is immunoreactive with polyclonal antiserum raised against Drosophila melanogaster casein kinase II (CKII). We have cloned, overexpressed and characterized a new member of the CKII family derived from Spodoptera frugiperda cells. Recombinant Sf9 CKII alpha subunit shares 75% identity to human, chicken and Drosophila melanogaster homologs, whereas the Sf9 CKII beta subunit is 77% identical to rat, chicken and human. Moreover, we demonstrate that the insect immunophilin FKBP46 can be phosphorylated by human and Sf9 casein kinase II. Finally, we show that FKBP46 interacts with DNA, and this interaction is not prevented by phosphorylation.

Amino Acid Sequence↗
PubMed1997

Expression of lacZ reporter gene under the control of the polyhedrin promoter of Spodoptera litura nuclear polyhedrosis virus.

Promoter function of the putative polyhedrin-encoding gene (polh) of Spodoptera litura nuclear polyhedrosis virus (S1MNPV) was determined by transferring it to the Autographa californica nuclear polyhedrosis virus (AcMNPV) through the AcNPV polh based vector, pVL1393. Three transfer vectors pCBT2, pCBT3 and pCBT4 were constructed by substituting the promoter and the neighbouring sequences of AcNPV in pVL1393 by that of S1NPV. The Escherichia coli lacZ gene was placed downstream from the S1NPV polh promoter in the hybrid transfer vector (pCBT) constructs. Co-transfection of Spodoptera frugiperda cells (Sf9) with each of the pCBTlacZ vector and wild-type AcNPV DNAs led to synthesis of beta-galactosidase (beta Gal). The plaque-purified recombinant viruses (S1AcNPV.lacZ) expressing lacZ under the polh promoter of S1NPV are stable. The highest beta Gal activity was obtained with S1AcNPV4.lacZ. Production of beta Gal with recombinant virus, S1AcNPV3.lacZ in which S1NPV polh promoter is in the reverse orientation in the AcNPV genome, is 83% of that produced by S1AcNPV4.lacZ. These results indicate that the S1NPV polh promoter is active in the genetic environment of AcNPV; the polh of S1NPV is phylogenetically related to AcNPV like other baculoviruses.

Animals↗
PubMed2001

Alpha-galactosidases from the larval midgut of Tenebrio molitor (Coleoptera) and Spodoptera frugiperda (Lepidoptera).

There are three midgut alpha-galactosidases (TG1, TG2, TG3) from Tenebrio molitor larvae that are partially resolved by ion-exchange chromatography. The enzymes have approximately the same pH optimum (5.0), pl value (4.6) and Mr value (46000-49000) as determined by gel filtration or native electrophoresis run in polyacrylamide gels with different concentrations. Substrate specificities and functions were proposed for the major T. molitor midgut alpha-galactosidases (TG2 and TG3) based on chromatographic, carbodiimide inactivation, Tris inhibition, and on substrate competition data. Thus, TG2 would hydrolyse alpha-1,6-galactosaccharides, exemplified by raffinose, whereas TG3 would act on melibiose and apparently also on digalactosyldiglyceride, the most important compound in the thylacoid membranes of chloroplasts. Most galactoside digestion should occur in the lumen of the first two thirds of T. molitor larval midguts, since alpha-galactosidase activity predominates there. Spodoptera frugiperda larvae have three midgut alpha-galactosidases (SG1, SG2, SG3) partially resolved by ion-exchange chromatography. The enzymes have similar pH optimum (5.8), pl value (7.2) and Mr value (46000-52000), and at least the major alpha-galactosidase must have an active carboxyl group in the active site. Based on data similar to those described for T. molitor, SG1 and SG3 should hydrolyse melibiose and SG3 should digest raffinose and, perhaps, also digalactosyldiglyceride. The midgut distribution of alpha-galactosidase activity supports the proposal that alpha-galactosidase digestion occurs at the surface of anterior midgut cells in Spodoptera frugiperda larvae.

Animals↗
PubMed2006

Morphological and molecular characterization of a new microsporidian (Protozoa: Microsporidia) isolated from Spodoptera litura (Fabricius) (Lepidoptera: Noctuidae).

A microsporidium was isolated from larvae of Spodoptera litura (Fabricius) collected from Tamil Nadu, India. This microsporidian species is monomorphic, disporous and develops in direct contact with the cytoplasm of the host cell. The nuclear configuration of merogonic and sporogonic stages was diplokaryotic. The merogonic proliferative stage was unusual that normal development with 1, 2 and 4 binucleated forms were common, while large multinucleate meronts containing 8 and 12 small compact horseshoe-like diplokaryotic nuclei were also observed. The fresh spores were typically ovocylindrical in shape, with a mean size of 3.91 x 1.91 microm and the polar filament length was approximately 90 microm. Infection was systemic with mature spores produced in the midgut, nervous tissue, muscles, labial glands, gonads, tracheae, epidermis, Malpighian tubules and, most extensively, fat body tissues. The new isolate was highly pathogenic to S. litura larvae. Host specificity tests performed on 37 non-target hosts of 5 different insect orders revealed that the new isolate is pathogenic only to lepidopteran insects. We sequenced the 16S small subunit rRNA (SSU rRNA) gene of the isolate and compared it with 72 non-redundant microsporidian sequences from the GenBank. Based on the light microscopic studies and phylogenetic analyses, the new isolate is assigned to the genus Nosema. Significant differences in the SSU rRNA sequence were identified when compared with the type species Nosema bombycis and other closely related species viz., Nosema spodopterae. Structural differences were also observed in the 16S SSU rRNA between the new isolate and the two above-mentioned microsporidian pathogens. We conclude that the microsporidian isolate reported here is distinctly different from the other known species and is likely to be a new species.

Animals↗
PubMed2003

Identification and classification of the Spodoptera littoralis nucleopolyhedrovirus inhibitor of apoptosis gene.

Baculoviruses possess two types of genes that suppressed apoptosis, p35 and inhibitor of apoptosis (iap). In this study we report the isolation and identification of an inhibitor of apoptosis gene Sliap in the genome of the Spodoptera littoralis nucleopolyhedrovirus (SINPV). The Sliap sequence predicted a 15 kDa polypeptide with only one BIR domain and a RING finger, both motifs characteristic of the IAP family of proteins, and a third specific acidic-rich motif. These characteristics, shared with the Spodoptera littura NPV IAP2/3, Epiphyas postvittana NPV IAP4, Lymantria dispar NPV IAP and Orgyia pseudotsugata NPV IAP4 (Orf 107) allowed us to classify them in a new homology group (IAP-4). Sliap was able to delay, but not to suppress, apoptosis induced by replication of a recombinant AcMNPV deficient in p35. In SINPV infected-SF9 cells Sliap was expressed earlier than sl-p49 suggesting that its role at the initiation of infection was to delay the apoptotic response of the host.

Amino Acid Sequence↗
PubMed2003

Sequence analysis of a 5.1 kbp region of the Spodoptera frugiperda multicapsid nucleopolyhedrovirus genome that comprises a functional ecdysteroid UDP-glucosyltransferase (egt) gene.

The ecdysteroid UDP-glucosyltransferase gene from the Spodoptera frugiperda multicapsid nucleopolyhedrovirus (SfMNPV) was identified using degenerate primers whose sequence were derived from conserved regions of the EGT proteins encoded by other baculoviruses. Analysis of the gene sequence revealed the presence of an open reading frame (ORF) with potential to encode a polypeptide of 525 amino acids. Promoter sequences typical of baculovirus genes were found in the 5' region of this ORF. A polyadenylation signal was identified downstream the translation stop codon. A transient expression assay showed that the product of this ORF was able to conjugate glucose from UDP-glucose with ecdysone confirming that the gene identified was indeed the SfMNPV egt gene. The SfMNPV egt gene and the sequences of other baculovirus egt genes were used to infer a phylogenetic tree. The nucleotide sequence of the entire BamHI fragment that contains the SfMNPV egt gene was determined. Search of the available sequence databases suggested that, besides the egt gene, this region contains 5 ORFs similar to the baculovirus genes gp37 (fusolin), to ptp2 and to ORFs 28, 29, and 30 of Spodoptera exigua multicapsid nucleopolyhedrovirus. Both the phylogenetic analysis of the egt genes and the gene order of the region that flanks the egt gene indicated that SfMNPV is closely related to the baculoviruses that infects S. exigua and Mamestra configurata.

Amino Acid Sequence↗
PubMed2003

Annotation pattern of ESTs from Spodoptera frugiperda Sf9 cells and analysis of the ribosomal protein genes reveal insect-specific features and unexpectedly low codon usage bias.

MOTIVATION: A whole set of Expressed Sequence Tags (ESTs) from the Sf9 cell line of Spodoptera frugiperda is presented here for the first time. By this way we want to identify both conserved and specific genes of this pest species. We also expect from this analysis to find a class of protein sequences providing a tool to explore genomic features and phylogeny of Lepidoptera. RESULTS: The ESTs display both housekeeping as well as developmentally regulated genes, and a high percentage of sequences with unknown function. Among the identified ORFs, almost all ribosomal proteins (RPs) were found with high EST redundancy and hence sequence accuracy. The codon usage found among RP genes is in average surprisingly much less biased in Lepidoptera than in other organisms. Other Spodoptera genes also displayed a low bias, suggesting a general genome expression feature in this Lepidoptera. We also found that the L35A and L36 RP sequences, respectively, display 40 and 10 amino-acid insertions, both being present only in insects. Sequence analysis suggests that they are probably not subjected to a strong selective pressure and may be good phylogenetic markers for Lepidoptera. Most interestingly, the Lepidoptera sequences of 9 RP genes displayed a specific signature different from the canonical one. We conclude that the RP family allows valuable comparative genomics and phylogeny of Lepidoptera. AVAILABILITY: All EST sequence data are available from the private 'Spodo-Base' upon request.

Abstracting and Indexing↗
PubMed1997

Identification and functional analysis of a non-hr origin of DNA replication in the genome of Spodoptera exigua multicapsid nucleopolyhedrovirus.

The genome of Spodoptera exigua multicapsid nucleopolyhedrovirus (SeMNPV) was screened for the presence of putative origins of DNA replication (oris). Using a transient DNA replication assay, several fragments were identified that underwent SeMNPV-dependent DNA replication in Spodoptera frugiperda cells (Sf-AE-21). Preliminary sequence data revealed the presence of multiple copies of homologous repeats (hrs). Restriction fragment Xbal-F2 showed a distinct sequence reminiscent of Autographa californica and Orgyla pseudotsugata MNPV (AcMNPV and OpMNPV) non-hr oris. Deletion analysis of this fragment indicated that the essential sequences of this putative non-hr ori mapped within a region of 800 bp. Sequence analysis of this region showed a unique distribution of six different (im)-perfect palindromes, several polyadenylation motifs and the occurrence of multiple direct repeats. No sequence homology or similarities to other reported baculovirus oris were detected. The spatial and modular distribution of these motifs are similar to those of the non-hr oris of AcMNPV and OpMNPV. Comparison of baculovirus non-hr and consensus eukaryotic oris revealed no consensus ori but indicated that each of the non-hrs studied so far is unique. From the structural similarity, however, it was concluded that the SeMNPV Xbal-F2 ori represents a baculovirus non-hr type ori. In addition, evidence is provided that SeMNPV renders more specificity to baculovirus DNA replication than AcMNPV.

Animals↗
PubMed1997

The p10 gene of Spodoptera littoralis nucleopolyhedrovirus: nucleotide sequence, transcriptional analysis and unique gene organization in the p10 locus.

The p10 gene of the Spodoptera littoralis (Spli) multicapsid nucleopolyhedrovirus (MNPV) was identified. With a coding sequence of 315 nucleotides (nt), corresponding to a protein of 104 amino acids, the SpliMNPV p10 gene is the longest p10 gene known. This gene codes for a putative protein with an Mr of 11130 and was found to be most closely related to the Spodoptera exigua (Se) MNPV p10 (49.4% amino acid identity) and most distant from the Autographa californica (Ac) MNPV p10 (20.0% amino acid identity). Characterization of the protein's secondary structure and a comparison with other p10 protein species suggested that this p10 has an extended alpha-helical domain with high probability of forming a large coiled-coil structure. The p10 mRNA was about 1500 nt long, as determined by Northern blot analysis. Primer extension assay mapped three transcription start sites to a conserved baculovirus late promoter motif, TAAG. In the SpliMNPV genome, the p10 gene is not flanked by genes similar to p26 and p74, as found in SeMNPV, AcMNPV, Choristoneura fumiferana MNPV and Orgyia pseudotsugata MNPV. Instead, an open reading frame (ORF) of 945 bp is located downstream from the p10 gene and is followed by another ORF in opposite orientation, encoding the p74 protein. Upstream of the p10 sequences, an ORF of 552 bp was identified that potentially encodes a 184 amino acid protein of Mr 20925, which showed 52.2% identity with the encoded product of the SeMNPV xb187 gene.

Amino Acid Sequence↗
PubMed1999

Identification and functional analysis of a putative non-hr origin of DNA replication from the Spodoptera littoralis type B multinucleocapsid nucleopolyhedrovirus.

A putative non-hr origin of DNA replication was identified in the Spodoptera littoralis multinucleocapsid nucleopolyhedrovirus (SpliNPV) genome by transient replication assays. The putative SpliNPV ori was mapped to the PstI-J fragment between 75.1-77.9 map units in the SpliNPV genome. While the DNA sequence of the putative SpliNPV ori aligned with regions within the non-hr oris of Autographa californica, Orgyia pseudotsugata and Spodoptera exigua multinucleocapsid nucleopolyhedroviruses, it has limited DNA sequence identity with these elements. The sequence of the putative SpliNPV non-hr ori fragment contains a unique distribution of imperfect palindromes, multiple direct repeats and putative transcription factor-binding sites. Transient expression assays indicated that the putative SpliNPV ori fragment repressed SpliNPV lef-3 promoter-mediated luciferase reporter gene expression. However, the putative SpliNPV ori fragment itself was capable of directing luciferase expression in the absence of a recognizable baculovirus promoter element in an orientation-independent fashion, suggesting that DNA sequence motifs within its sequence can activate transcription. Gel mobility shift analyses confirmed that proteins within nuclear extracts from both uninfected and virus-infected cells bound with specificity to the putative SpliNPV ori fragment.

Animals↗
PubMed2005

Spodoptera frugiperda resistance to oral infection by Autographa californica multiple nucleopolyhedrovirus linked to aberrant occlusion-derived virus binding in the midgut.

Spodoptera frugiperda larvae are highly resistant to oral infection by Autographa californica multiple nucleopolyhedrovirus (AcMNPV) (LD(50), approximately 9200 occlusions), but extremely susceptible to budded virus within the haemocoel (LD(50), <1 p.f.u.). The inability of AcMNPV occlusion-derived virus (ODV) to establish primary infections readily within midgut cells accounts for a major proportion of oral resistance. To determine whether inappropriate binding of AcMNPV ODV to S. frugiperda midgut cells contributes to lack of oral infectivity, the binding and fusion properties of AcMNPV ODV were compared with those of the ODV of a new isolate of Spodoptera frugiperda multiple nucleopolyhedrovirus (SfMNPV) obtained from a field-collected larva (oral LD(50), 12 occlusions). By using a fluorescence-dequenching assay conducted in vivo, it was found that AcMNPV ODV bound to the midgut epithelia of S. frugiperda larvae at approximately 15 % of the level of SfMNPV ODV, but that, once bound, the efficiencies of fusion for the two ODVs were similar: 60 % for AcMNPV and 53 % for SfMNPV. Whilst the difference in binding efficiencies was significant, it could not account entirely for the observed differences in infectivity. Competition experiments, however, revealed that, in S. frugiperda larvae, SfMNPV ODV bound to a midgut cell receptor that was not bound by AcMNPV ODV, indicating that ODV interaction with a specific receptor(s) was necessary for productive infection of midgut columnar epithelial cells. Fusion in the absence of this ligand-receptor interaction did not result in productive infections.

Animals↗
PubMed1999

Isolation of an apoptosis suppressor gene of the Spodoptera littoralis nucleopolyhedrovirus.

Spodoptera frugiperda SF9 cells infected with mutants of the Autographa californica nucleopolyhedrovirus (AcMNPV) which lack a functional p35 gene undergo apoptosis, aborting the viral infection. The Spodoptera littoralis nucleopolyhedrovirus (SlNPV) was able to suppress apoptosis triggered by vDeltaP35K/pol+, an AcMNPV p35 null mutant. To identify the putative apoptotic suppressor gene of SlNPV, overlapping cosmid clones representing the entire SlNPV genome were individually cotransfected along with genomic DNA of vDeltaP35K/pol+. Using this complementation assay, we isolated a SlNPV DNA fragment that was able to rescue the vDeltaP35K/pol+ infection in SF9 cells. By further subcloning and rescue, we identified a novel SlNPV gene, Slp49. The Slp49 sequence predicted a 49-kDa polypeptide with about 48.8% identity to the AcMNPV apoptotic suppressor P35. SLP49 displays a potential recognition site, TVTDG, for cleavage by death caspases. Recombinant AcMNPVs deficient in p35 bearing the Slp49 gene did not induce apoptosis and showed successful productive infections in SF9 cells, indicating that Slp49 is a functional homologue of p35. A 1.5-kbp Slp49-specific transcript was identified in SF9 cells infected with SlNPV or with vAc496, a vDeltaP35K/pol+-recombinant bearing Slp49. The discovery of Slp49 contributes to the identification of important functional motifs conserved in p35-like apoptotic suppressors and to the future isolation of p35-like genes from other baculoviruses.

Amino Acid Sequence↗
PubMed2003

Specific incorporation of L-glutamine into volicitin in the regurgitant of Spodoptera litura.

Volicitin, [N-(17-hydroxylinolenoyl)-L-glutamine], was identified as an elicitor of plant volatiles from a Spodoptera exigua regurgitant. It has been proposed that gut microbes synthesize volicitin from glutamine, a predominant amino acid component in the insect gut. However, we found that glutamine was not a major component in the regurgitant of Spodoptera litura, although L-glutamine was exclusively incorporated into volicitin by S. litura fed on diets enriched with various amino acids. This selectivity of glutamine as a substrate was not due to a dominant occurrence in the insect gut.

Amino Acids↗
PubMed1999

Characterization of the ecdysteroid UDP-glucosyltransferase gene of Spodoptera litura multinucleocapsid nucleopolyhedrovirus.

The ecdysteroid UDP-glucosyltransferase (EGT) gene of Spodoptera litura multinucleocapsid nucleopolyhedrovirus (SpltMNPV), Guangzhouisolate was sequenced. The open reading frame of the gene is 1530 nucleotides long, encoding a putative protein of 509 amino acids with Mr of 58,500. The 5' noncoding region has a TATA box. A polyadenylation signal, AATAAA, is contained downstream of the translation stop codon. A putative signal peptide is present at the N-terminus of the protein. Homology comparison with other baculovirus egt genes showed that these genes are highly conserved. The SpltMNPV egt gene is closely related to that of Spodoptera littoralis nucleopolyhedrovirus (SliNPV) with the identities of 84% in nucleotide and 91% in amino acid, respectively. In this study, an alignment of amino acid sequences has been made and a tentative phylogenetic tree of twelve baculovirus egts is presented.

Amino Acid Sequence↗