Characterization of Spodoptera exigua multicapsid nucleopolyhedrovirus ORF17/18, a homologue of Xestia c-nigrum granulovirus ORF129

IJkel, W.F.J.; Roode, Els C.; Goldbach, Rob; Vlak, Just M.; Zuidema, D.

doi:10.1099/0022-1317-83-11-2857

Cited by 2 publications

(1 citation statement)

References 40 publications

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“…Dm-cF mRNA and protein were not detected in embryos, first or second instar larvae, but they were detected in third instar larvae and in adults. Because some viral F proteins go through a cleavagematuration step that produces two distinct subfragments and activates the fusion function (21,42,49), we also examined Dm-cF for similar proteolytic cleavage. When Dm-cF was transiently expressed in S2 cells, a protein of the size predicted for full-length Dm-cF was identified, and no discernible cleavage was detected.…”

Section: Discussionmentioning

confidence: 99%

A Cellular Drosophila melanogaster Protein with Similarity to Baculovirus F Envelope Fusion Proteins

Lung

Blissard

2005

J Virol

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Baculovirus F (fusion) proteins are found in the envelopes of budded virions. Recently a Drosophila melanogaster gene (CG4715) that encodes a protein with sequence similarity to baculovirus F proteins was discovered. To examine similarities and differences with baculovirus F proteins, we cloned the D. melanogaster cellular F (Dm-cF) protein gene and analyzed Dm-cF expression and localization. The predicted Dm-cF protein sequence lacks a furin cleavage site, and transiently expressed Dm-cF showed no protein cleavage and no detectable membrane fusion activity. In cell localization studies, transiently expressed Dm-cF was localized to intracellular organelles in D. melanogaster S2 cells, unlike baculovirus F proteins, which localize to cellular plasma membranes. Using reverse transcriptase PCR and Western blot analysis to examine Dm-cF expression in animals, we detected Dm-cF expression in both larval and adult D. melanogaster cells. However, Dm-cF expression was detected only in third instar larvae and adults, suggesting that Dm-cF expression may be developmentally regulated. We also identified genes related to Dm-cF in the genomes of two other Drosophila species, Drosophila yakuba and Drosophila pseudoobscura, and the mosquito Anopheles gambiae. These observations suggest that f genes may be present in the genomes of many insects. Conservation within and between 22 baculovirus and 4 insect F proteins was examined in detail. These studies demonstrate that Dm-cF is expressed in D. melanogaster and suggest that if baculovirus f genes are derived from a host cellular f gene, the function appears to have changed substantially upon adaptation to the baculovirus infection cycle.

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Section: Discussionmentioning

confidence: 99%

A Cellular Drosophila melanogaster Protein with Similarity to Baculovirus F Envelope Fusion Proteins

Lung

Blissard

2005

J Virol

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Prediction of functional class of novel viral proteins by a statistical learning method irrespective of sequence similarity

Han

Cai

et al. 2005

Virology

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The function of a substantial percentage of the putative protein-coding open reading frames (ORFs) in viral genomes is unknown. As their sequence is not similar to that of proteins of known function, the function of these ORFs cannot be assigned on the basis of sequence similarity. Methods complement or in combination with sequence similarity-based approaches are being explored. The web-based software SVMProt (http://jing.cz3.nus.edu.sg/cgi-bin/svmprot.cgi) to some extent assigns protein functional family irrespective of sequence similarity and has been found to be useful for studying distantly related proteins [Cai, C.Z., Han, L.Y., Ji, Z.L., Chen, X., Chen, Y.Z., 2003. SVM-Prot: web-based support vector machine software for functional classification of a protein from its primary sequence. Nucleic Acids Res. 31(13): 3692-3697]. Here 25 novel viral proteins are selected to test the capability of SVMProt for functional family assignment of viral proteins whose function cannot be confidently predicted on by sequence similarity methods at present. These proteins are without a sequence homolog in the Swissprot database, with its precise function provided in the literature, and not included in the training sets of SVMProt. The predicted functional classes of 72% of these proteins match the literature-described function, which is compared to the overall accuracy of 87% for SVMProt functional class assignment of 34582 proteins. This suggests that SVMProt to some extent is capable of functional class assignment irrespective of sequence similarity and it is potentially useful for facilitating functional study of novel viral proteins.

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Characterization of Spodoptera exigua multicapsid nucleopolyhedrovirus ORF17/18, a homologue of Xestia c-nigrum granulovirus ORF129

Cited by 2 publications

References 40 publications

A Cellular Drosophila melanogaster Protein with Similarity to Baculovirus F Envelope Fusion Proteins

A Cellular Drosophila melanogaster Protein with Similarity to Baculovirus F Envelope Fusion Proteins

Prediction of functional class of novel viral proteins by a statistical learning method irrespective of sequence similarity

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