The crystal structure of novel chondroitin lyase ODV‐E66, a baculovirus envelope protein

Kawaguchi, Yoshirou; Sugiura, Norío; Kimata, Koji; Kimura, Makoto; Kakuta, Yoshimitsu

doi:10.1016/j.febslet.2013.10.021

Cited by 15 publications

(13 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, despite their homology, PmNV034 and PmNV036 have different lengths, relatively low identity and similarity (38% and 53%, respectively), and the hydrophobic INM-sorting sequence was found only in PmNV036 and not in PmNV034. AcMNPV ODV-E66 has also recently been shown to act as a chondroitin lyase [44]. Interestingly, both PmNV034 and PmNV036 contain all five of the conserved catalytic residues that are found in AcMNPV ODV-E66, suggesting that either or both of these proteins might function as a chondroitin lyase.…”

Section: Resultsmentioning

confidence: 99%

The genome and occlusion bodies of marine Penaeus monodon nudivirus (PmNV, also known as MBV and PemoNPV) suggest that it should be assigned to a new nudivirus genus that is distinct from the terrestrial nudiviruses

et al. 2014

View full text Add to dashboard Cite

BackgroundPenaeus monodon nudivirus (PmNV) is the causative agent of spherical baculovirosis in shrimp (Penaeus monodon). This disease causes significant mortalities at the larval stage and early postlarval (PL) stage and may suppress growth and reduce survival and production in aquaculture. The nomenclature and classification status of PmNV has been changed several times due to morphological observation and phylogenetic analysis of its partial genome sequence. In this study, we therefore completed the genome sequence and constructed phylogenetic trees to clarify PmNV’s taxonomic position. To better understand the characteristics of the occlusion bodies formed by this marine occluded virus, we also compared the chemical properties of the polyhedrin produced by PmNV and the baculovirus AcMNPV (Autographa californica nucleopolyhedrovirus).ResultsWe used next generation sequencing and traditional PCR methods to obtain the complete PmNV genome sequence of 119,638 bp encoding 115 putative ORFs. Phylogenetic tree analysis showed that several PmNV genes and sequences clustered with the non-occluded nudiviruses and not with the baculoviruses. We also investigated the characteristics of PmNV polyhedrin, which is a functionally important protein and the major component of the viral OBs (occlusion bodies). We found that both recombinant PmNV polyhedrin and wild-type PmNV OBs were sensitive to acid conditions, but unlike the baculoviral OBs, they were not susceptible to alkali treatment.ConclusionsFrom the viral genome features and phylogenetic analysis we conclude that PmNV is not a baculovirus, and that it should be assigned to the proposed Nudiviridae family with the other nudiviruses, but into a distinct new genus (Gammanudivirus).Electronic supplementary materialThe online version of this article (doi:10.1186/1471-2164-15-628) contains supplementary material, which is available to authorized users.

show abstract

Section: Resultsmentioning

confidence: 99%

The genome and occlusion bodies of marine Penaeus monodon nudivirus (PmNV, also known as MBV and PemoNPV) suggest that it should be assigned to a new nudivirus genus that is distinct from the terrestrial nudiviruses

et al. 2014

View full text Add to dashboard Cite

show abstract

“…We identified PrDs in 56 out of 66 known species belonging this family, indicating that this high prevalence of PrDs in one viral family may not be a coincidence. Therefore, we further showed that one of the PrDs associated with the cell adhesion and entry most frequently found in Baculoviridae is occlusion-derived virus envelope protein 66 (ODV-E66), which was recently the first identified viral chondroitin lyase, an enzyme that degrades chondroitin and is associated with viral entry 65,66 .…”

Section: Discussionmentioning

confidence: 97%

Prion-like Domains in Eukaryotic Viruses

Tetz

2018

Sci Rep

View full text Add to dashboard Cite

Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition to the previously demonstrated pathogenic roles of prions during the development of different mammalian diseases, including neurodegenerative diseases, they have recently been shown to represent an important functional component in many prokaryotic and eukaryotic organisms and bacteriophages, confirming the previously unexplored important regulatory and functional roles. However, an in-depth analysis of these domains in eukaryotic viruses has not been performed. Here, we examined the presence of prion-like proteins in eukaryotic viruses that play a primary role in different ecosystems and that are associated with emerging diseases in humans. We identified relevant functional associations in different viral processes and regularities in their presence at different taxonomic levels. Using the prion-like amino-acid composition computational algorithm, we detected 2679 unique putative prion-like domains within 2,742,160 publicly available viral protein sequences. Our findings indicate that viral prion-like proteins can be found in different viruses of insects, plants, mammals, and humans. The analysis performed here demonstrated common patterns in the distribution of prion-like domains across viral orders and families, and revealed probable functional associations with different steps of viral replication and interaction with host cells. These data allow the identification of the viral prion-like proteins as potential novel regulators of viral infections.

show abstract

“…The results of x-ray crystallography studies pertaining to GAG eliminase and its enzyme-substrate complexes have allowed for the molecular mechanisms of polysaccharide degradation to be elucidated, as well as providing information concerning the potential direction of the reaction (16,22,36,37,39). However, the lack of conclusive evidence to support the direction of this process means that the direction currently remains unclear, which is primarily due to a lack of appropriate homologous model substrates.…”

Section: Resultsmentioning

confidence: 99%

Uncovering the Catalytic Direction of Chondroitin AC Exolyase

Yin

Wang

Sheng

2016

Journal of Biological Chemistry

View full text Add to dashboard Cite

Glycosaminoglycans (GAGs) are polysaccharides that play vital functional roles in numerous biological processes, and compounds belonging to this class have been implicated in a wide variety of diseases. Chondroitin AC lyase (ChnAC) (EC 4.2.2.5) catalyzes the degradation of various GAGs, including chondroitin sulfate and hyaluronic acid, to give the corresponding disaccharides containing an ⌬ 4 -unsaturated uronic acid at their non-reducing terminus. ChnAC has been isolated from various bacteria and utilized as an enzymatic tool for study and evaluating the sequencing of GAGs. Despite its substrate specificity and the fact that its crystal structure has been determined to a high resolution, the direction in which ChnAC catalyzes the cleavage of oligosaccharides remain unclear. Herein, we have determined the structural cues of substrate depolymerization and the cleavage direction of ChnAC using model substrates and recombinant ChnAC protein. Several structurally defined oligosaccharides were synthesized using a chemoenzymatic approach and subsequently cleaved using ChnAC. The degradation products resulting from this process were determined by mass spectrometry. The results revealed that ChnAC cleaved the ␤1,4-glycosidic linkages between glucuronic acid and glucosamine units when these bonds were located on the reducing end of the oligosaccharide. In contrast, the presence of a GlcNAc-␣-1,4-GlcA unit at the reducing end of the oligosaccharide prevented ChnAC from cleaving the GalNAc-␤1,4-GlcA moiety located in the middle or at the non-reducing end of the chain. These interesting results therefore provide direct proof that ChnAC cleaves oligosaccharide substrates from their reducing end toward their non-reducing end. This conclusion will therefore enhance our collective understanding of the mode of action of ChnAC.

show abstract

The crystal structure of novel chondroitin lyase ODV‐E66, a baculovirus envelope protein

Cited by 15 publications

References 41 publications

The genome and occlusion bodies of marine Penaeus monodon nudivirus (PmNV, also known as MBV and PemoNPV) suggest that it should be assigned to a new nudivirus genus that is distinct from the terrestrial nudiviruses

The genome and occlusion bodies of marine Penaeus monodon nudivirus (PmNV, also known as MBV and PemoNPV) suggest that it should be assigned to a new nudivirus genus that is distinct from the terrestrial nudiviruses

Prion-like Domains in Eukaryotic Viruses

Uncovering the Catalytic Direction of Chondroitin AC Exolyase

Contact Info

Product

Resources

About