Glycosyltransferases encoded by viruses

Markine-Goriaynoff, Nicolas; Gillet, Laurent; Etten, James L. Van; Korres, Haralambos; Verma, Naresh K.; Vanderplasschen, Alain

doi:10.1099/vir.0.80320-0

Cited by 105 publications

(102 citation statements)

References 147 publications

Supporting

Mentioning

101

Contrasting

Order By: Relevance

“…Unlike other viruses, PBCV-1 encodes at least part, if not all, of the machinery required to glycosylate its major capsid protein (19), including five glycosyltransferases (11, 38, 43). Further- more, glycosylation of the virus major capsid protein probably occurs independently of the host endoplasmic reticulum-Golgi system (19). All of the glycosyltransferase CDSs were expressed early (A64R, A111/114R, A219/222/226R, A473L, and A546L).…”

Section: Resultsmentioning

confidence: 99%

Microarray Analysis of Paramecium bursaria Chlorella Virus 1 Transcription

Yanai-Balser

Duncan

Eudy

et al. 2010

J Virol

Self Cite

View full text Add to dashboard Cite

Paramecium bursaria chlorella virus 1 (PBCV-1), the prototype of the genus Chlorovirus (family Phycodnaviridae), is a large, icosahedral (190 nm in diameter), plaque-forming virus that infects the unicellular, eukaryotic green alga Chlorella sp. strain NC64A. The PBCV-1 virion has a lipid membrane located inside an outer glycoprotein capsid. The 330-kb genome is a linear, nonpermutated, double-stranded DNA (dsDNA) molecule with covalently closed hairpin ends that has approximately 365 protein encoding genes (CDSs), as well as 11 tRNA encoding genes (reviewed in references 34, 39, and 40). The CDSs are evenly distributed on both strands and intergenic space is minimal (typically fewer than 100 nucleotides); the exception is a 1,788-bp sequence in the middle of the genome that encodes the tRNA genes. Approximately 35% of the 365 PBCV-1 gene products resemble proteins in the public databases.PBCV-1 initiates infection by attaching rapidly and specifically to the cell wall of its host (22), probably at a unique virus vertex (4, 26). Attachment is immediately followed by host cell wall degradation by a virus-packaged enzyme(s) at the point of contact. After wall degradation, the viral internal membrane presumably fuses with the host membrane, causing host membrane depolarization (9), potassium ion efflux (25), and an increase in the cytoplasm pH (2). These events are predicted to facilitate entry of the viral DNA and virion-associated proteins into the cell. PBCV-1 lacks a gene encoding a recognizable RNA polymerase or a subunit of it, and RNA polymerase activity is not detected in PBCV-1 virions. Therefore, viral DNA and virion-associated proteins are predicted to migrate to the nucleus, and early viral transcription is detected 5 to 10 min postinfection (p.i.), presumably by commandeering a host RNA polymerase(s) (possibly RNA polymerase II) (14, 29). Virus DNA synthesis begins 60 to 90 min p.i., followed by virus assembly at 3 to 5 h p.i. in localized regions of the cytoplasm, called virus assembly centers (21). At 6 to 8 h p.i., virusinduced host cell lysis occurs resulting in release of progeny virions (ϳ1,000 viruses/cell, ϳ25% of which are infectious). These events are depicted in Fig. 1.To initiate PBCV-1 transcription, the host RNA polymerase(s), possibly in combination with a virus transcription factor(s), must recognize virus DNA promoter sequences. Recently, three short nucleotide sequences were identified in putative virus promoter regions (150 bp upstream and 50 bp downstream of the ATG translation site) that are conserved in PBCV-1 and other Chlorovirus members (7). PBCV-1 CDSs are not spatially clustered on the genome by either temporal or functional class, suggesting that transcription regulation must occur via cis-and possible trans-acting regulatory elements.To understand the dynamics of PBCV-1 global gene expression during virus replication, we constructed a microarray containing 50-mer probes to each of the 365 PBCV-1 CDSs.

show abstract

Section: Resultsmentioning

confidence: 99%

Microarray Analysis of Paramecium bursaria Chlorella Virus 1 Transcription

Yanai-Balser

Duncan

Eudy

et al. 2010

J Virol

Self Cite

View full text Add to dashboard Cite

show abstract

“…These enzymes presumably contribute to the formation of specific glycan structures, which differ from those in host cells and which contribute to virus infectivity. This property differs from those of most viruses, which use the host ER/Golgi system for glycosylation of their surface proteins and whose glycan structure and composition are completely dependent on their host cells (30). The glycans produced by the virus PBCV-1, which infects Chlorella sp.…”

Section: Discussionmentioning

confidence: 96%

“…They have large genomes that often encode genes not commonly found in viruses. For example, several lines of evidence indicate that Paramecium bursaria chlorella virus 1 (PBCV-1) and other chlorovirus members, such as Acanthocystis turfacea chlorella virus 1 (ATCV-1), encode at least part, if not all, of the machinery required to glycosylate their structural proteins, including glycosyltransferases (13,21,30,33,(41)(42)(43). Furthermore, glycosylation occurs independently of the host endoplasmic reticulum (ER)-Golgi system (33,(42)(43)(44).…”

mentioning

confidence: 99%

Identification of an l -Rhamnose Synthetic Pathway in Two Nucleocytoplasmic Large DNA Viruses

Chothi

Duncan

Armirotti

et al. 2010

J Virol

Self Cite

View full text Add to dashboard Cite

“…The large genomes of phycodnaviruses harbor genes that are unusual for viruses. Paramecium bursaria chlorella virus 1 (PBCV-1), for example, is capable of constructing complex oligosaccharides independent of its host (Markine-Goriaynoff et al, 2004). EhV-86, a coccolithovirus, encodes genes involved in the synthesis of sphingolipids (Wilson et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Detection of inteins among diverse DNA polymerase genes of uncultivated members of the Phycodnaviridae

2008

View full text Add to dashboard Cite

Viruses in the family Phycodnaviridae infect autotrophic protists in aquatic environments. Application of a PCR assay targeting the DNA polymerase of viruses in this family has revealed that phycodnaviruses are quite diverse and appear to be widespread, but a limited number of environments have been examined so far. In this study, we examined the sequence diversity among viral DNA pol genes amplified by PCR from subtropical coastal waters of O'ahu, Hawai'i. A total of 18 novel prasinovirus-like sequences were detected along with two other divergent sequences that differ at the genus-level relative to other sequences in the family. Of the 20 new sequence types reported here, three were serendipitously found to contain protein introns, or inteins. Sequence analysis of the inteins suggested that all three have self-splicing domains and are apparently capable of removing themselves from the translated polymerase protein. Two of the three also appear to be 'active', meaning they encode all the motifs necessary for a complete dodecapeptide homing endonuclease, and are therefore capable of horizontal transfer. A subsequent PCR survey of our samples with intein-specific primers suggested that intein-containing phycodnaviruses are common in this environment. A search for similar sequences in metagenomic data sets from other oceans indicated that viral inteins are also widespread, but how these genetic parasites might be influencing the ecology and evolution of phycodnaviruses remains unclear.

show abstract

Glycosyltransferases encoded by viruses

Cited by 105 publications

References 147 publications

Microarray Analysis of Paramecium bursaria Chlorella Virus 1 Transcription

Microarray Analysis of Paramecium bursaria Chlorella Virus 1 Transcription

Identification of an l -Rhamnose Synthetic Pathway in Two Nucleocytoplasmic Large DNA Viruses

Detection of inteins among diverse DNA polymerase genes of uncultivated members of the Phycodnaviridae

Contact Info

Product

Resources

About