Identification and expression of two baculovirus gp37 genes.

Phanis, C. G.; Miller, Davin; Cassar, Steven; Tristem, Michael; Thiem, Suzanne M.; O’Reilly, David R.

doi:10.1099/0022-1317-80-7-1823

Cited by 30 publications

(26 citation statements)

References 39 publications

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“…The baculovirus-homologous ORF (clone A526) is also of special interest. This ORF is homologous to fusolin (also known as spindle-body protein or GP37 [38]). Fusolin has been found in baculoviruses and in insectinfecting poxviruses and has been shown to enhance infection by a factor of 10 4 .…”

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Phytoplasmal Genes, Employing a Novel Method of Isolating Phytoplasmal Genomic DNA

et al. 2003

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Phytoplasmas are unculturable, insect-transmissible plant pathogens belonging to the class Mollicutes. To be transmitted, the phytoplasmas replicate in the insect body and are delivered to the insect's salivary glands, from where they are injected into the recipient plant. Because phytoplasmas cannot be cultured, any attempt to recover phytoplasmal DNA from infected plants or insects has resulted in preparations with a large background of host DNA. Thus, studies of the phytoplasmal genome have been greatly hampered, and aside from the rRNA genes, only a few genes have hitherto been isolated and characterized. We developed a unique method to obtain host-free phytoplasmal genomic DNA from the insect vector's saliva, and we demonstrated the feasibility of this method by isolating and characterizing 78 new putative phytoplasmal open reading frames and their deduced proteins. Based on the newly accumulated information on phytoplasmal genes, preliminary characteristics of the phytoplasmal genome are discussed.

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Section: Discussionmentioning

confidence: 99%

Identification and Characterization of Phytoplasmal Genes, Employing a Novel Method of Isolating Phytoplasmal Genomic DNA

et al. 2003

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“…The C-terminal regions of EPV fusolins are not conserved and are variable in length (5,20,34). Intriguingly, in this study, the C-terminal region was eliminated by a serine protease(s) in digestive juice.…”

Section: Discussionmentioning

confidence: 68%

“…The N-terminal region of the mature fusolin (ca. 230 amino acids) contains five discrete and highly conserved sequence elements, and these elements form a putative chitin-binding domain (5,20,28,34,40). Although the chitin-binding ability of the EPV fusolins has not yet been demonstrated, it is thought to be crucial for PM disintegration, since chitin is a constituent of the PM (20,22).…”

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confidence: 99%

The N-Terminal Region of an Entomopoxvirus Fusolin Is Essential for the Enhancement of Peroral Infection, whereas the C-Terminal Region Is Eliminated in Digestive Juice

Takemoto

Mitsuhashi

Murakami

et al. 2008

J Virol

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The spindles of Anomala cuprea entomopoxvirus (AncuEPV), which are composed of glycoprotein fusolin, are known to enhance the peroral infectivity of AncuEPV itself and of nucleopolyhedroviruses. This has been demonstrated to involve the disruption of intestinal peritrophic membrane (PM), composed of chitin matrix, glycosaminoglycans, and proteins. To identify essential and nonessential regions for this enhancement activity, AncuEPV fusolin and its deletion mutants were expressed in Sf21 cells using a baculovirus system, and their enhancement abilities were analyzed. The recombinant fusolin enhanced the peroral infectivity of Bombyx mori nucleopolyhedrovirus up to 320-fold and facilitated the infection of host insect with AncuEPV. Deletion mutagenesis revealed that the N-terminal region (amino acids 1 to 253), a possible chitin-binding domain, is essential for the enhancement of infection, whereas the C-terminal region is entirely dispensable. The glycosylation-defective mutants N191Q, whose Asn 191 is replaced with Gln, and ⌬SIG, whose signal peptide is deleted, showed considerably reduced and abolished enhancing activities, respectively, indicating that the carbohydrate chain is important in the enhancing activity. Interestingly, the C-terminal dispensable region was digested by a serine protease(s) in insect digestive juice. Moreover, both the N-terminal conserved region and the carbohydrate chain were necessary not only for chitin binding but also for stability in digestive juice. A triple amino acid replacement mutant, IHE (Ile-His-Glu 161 to Ala-Ala-Ala), was stable in digestive juice and had chitin-binding ability but did not retain its enhancing activity. These results suggest that the enhancement of infectivity involves more than the tolerance to digestive juice and chitin-binding ability.

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“…The phylogenetic tree of ubiquitin from this study was compared with other evolutionary trees from previous studies such as GP37 (Phanis et al, 1999), UDP glucuronosyltransferase, Chi, inhibitor of apoptosis (Hairong, 2011), alk-exo (Keeling and Palmer, 2008), and DNA polymerase (Herniou et al, 2003). According to the position of the ubiquitin gene in baculovirus, 3 upstream and 3 downstream sequences were found.…”

Section: Discussionmentioning

confidence: 99%

Evolutionary analysis of the ubiquitin gene of baculovirus and insect hosts

Ma¹,

Zhang²,

Xia³

et al. 2015

Genet. Mol. Res.

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ABSTRACT.Baculovirus is the only virus that has been found to encode the ubiquitin protein. In this study, ubiquitin sequences from 16 insects and 49 viruses were collected and compared. The resulting sequences were aligned with virus genomes. Then MAGE 5.0, k-estimated software, as well as other software programs were used for systemic evolutionary, selection pressure, and evolutionary distance analysis. The results of the pairwise ratio of non-synonymous to synonymous substitution values and evolutionary distances showed that ubiquitin from baculovirus and insect hosts have been under purifying selection during evolution and are thus evolutionarily conserved. Moreover, genes from insect hosts were more conserved than those in baculovirus. Analysis of the non-synonymous to synonymous substitution rates at each site and entropy calculations revealed the evolutionary status of every site in the ubiquitin genes of baculovirus and their hosts. Genome locations and phylogenetic trees indicated that granuloviruses and non-photosynthetic vegetation evolved, and granulovirus evolution was more similar to that of insect hosts. Our results suggest that the ubiquitin gene in baculovirus may have been acquired through horizontal transfer from the host.

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Identification and expression of two baculovirus gp37 genes.

Cited by 30 publications

References 39 publications

Identification and Characterization of Phytoplasmal Genes, Employing a Novel Method of Isolating Phytoplasmal Genomic DNA

Identification and Characterization of Phytoplasmal Genes, Employing a Novel Method of Isolating Phytoplasmal Genomic DNA

The N-Terminal Region of an Entomopoxvirus Fusolin Is Essential for the Enhancement of Peroral Infection, whereas the C-Terminal Region Is Eliminated in Digestive Juice

Evolutionary analysis of the ubiquitin gene of baculovirus and insect hosts

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