Giant viruses of the<i>Megavirinae</i>subfamily possess biosynthetic pathways to produce rare bacterial-like sugars in a clade-specific manner

Notaro, Anna; Poirot, Olivier; Garcin, Elsa D.; Nin, Sébastien; Molinaro, Antonio; Tonetti, Michela; Castro, Cristina De; Abergel, Chantal

doi:10.1093/femsml/uqac002

Cited by 11 publications

(49 citation statements)

References 71 publications

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“…In PBCV-1, the prototype of the Chloroviruses , the glycogenes are mostly scattered throughout the genome, with a majority in the first 100 ORFs, making it difficult to define a specific region responsible for the glycosylation of the viral capsid protein. In contrast, glycogenes in the Megavirinae subfamily occur in specific regions of the genome, defining complex clusters of six to as many as 33 genes . The next sections will describe the sugar nucleotide biosynthetic pathways that have been experimentally validated for Megavirinae , together with a few inferred from in silico analysis.…”

Section: Biosynthetic Machinery and The Glycans Produced By Giant Vir...mentioning

confidence: 79%

“…In contrast, glycogenes in the Megavirinae subfamily occur in specific regions of the genome, defining complex clusters of six to as many as 33 genes. 87 The next sections will describe the sugar nucleotide biosynthetic pathways that have been experimentally validated for Megavirinae, together with a few inferred from in silico analysis.…”

Section: Biosynthesis Of the Udp-β-l-rha Precursor In Atcv-1mentioning

confidence: 99%

“…This study also analyzed the genome of 55 fully sequenced viruses in five clades and combined the results of the bioinformatic predictions with the experimental data, either acquired in the same work or taken from previous studies. 87 The protein sequences of well-annotated glycogenes were used as input to search for homologous proteins in the genome of each virus. Multiple alignments were performed to assess the conservation level of the active sites and consequently the functionality of the enzymes.…”

Section: Apmv Udp-α-d-glcnacmentioning

confidence: 99%

“…Finally, the existence of this great variability in the glycosylation machinery of the different clades suggests that glycans contribute to the fitness of the viruses in the environment, where they have to compete with bacteria and other giant viruses for the same host. 87 Clade A. Analysis of this clade involved 28 different strains, with APMV as the prototype.…”

Section: Apmv Udp-α-d-glcnacmentioning

confidence: 99%

“…With regard to glyco-related genes, all of the members of this genus encode for several GTs and other enzymes involved in sugar metabolism, as discussed in section …”

Section: Nucleocytoplasmic Large Dna Virusesmentioning

confidence: 99%

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The Astounding World of Glycans from Giant Viruses

Speciale¹,

Notaro

Abergel

et al. 2022

Chem. Rev.

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Viruses are a heterogeneous ensemble of entities, all sharing the need for a suitable host to replicate. They are extremely diverse, varying in morphology, size, nature, and complexity of their genomic content. Typically, viruses use host-encoded glycosyltransferases and glycosidases to add and remove sugar residues from their glycoproteins. Thus, the structure of the glycans on the viral proteins have, to date, typically been considered to mimick those of the host. However, the more recently discovered large and giant viruses differ from this paradigm. At least some of these viruses code for an (almost) autonomous glycosylation pathway. These viral genes include those that encode the production of activated sugars, glycosyltransferases, and other enzymes able to manipulate sugars at various levels. This review focuses on large and giant viruses that produce carbohydrate-processing enzymes. A brief description of those harboring these features at the genomic level will be discussed, followed by the achievements reached with regard to the elucidation of the glycan structures, the activity of the proteins able to manipulate sugars, and the organic synthesis of some of these virus-encoded glycans. During this progression, we will also comment on many of the challenging questions on this subject that remain to be addressed. CONTENTS AJ 4.2. Chlorovirus N-Glycans AJ 5. Conclusions and Future Perspectives AN Author Information

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Section: Biosynthetic Machinery and The Glycans Produced By Giant Vir...mentioning

confidence: 79%

Section: Biosynthesis Of the Udp-β-l-rha Precursor In Atcv-1mentioning

confidence: 99%

Section: Apmv Udp-α-d-glcnacmentioning

confidence: 99%

Section: Apmv Udp-α-d-glcnacmentioning

confidence: 99%

“…With regard to glyco-related genes, all of the members of this genus encode for several GTs and other enzymes involved in sugar metabolism, as discussed in section …”

Section: Nucleocytoplasmic Large Dna Virusesmentioning

confidence: 99%

See 3 more Smart Citations

The Astounding World of Glycans from Giant Viruses

Speciale¹,

Notaro

Abergel

et al. 2022

Chem. Rev.

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Polysaccharide sulfotransferases: the identification of putative sequences and respective functional characterisation

Mistry,

Byrne,

Starns

et al. 2024

Essays in Biochemistry

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The vast structural diversity of sulfated polysaccharides demands an equally diverse array of enzymes known as polysaccharide sulfotransferases (PSTs). PSTs are present across all kingdoms of life, including algae, fungi and archaea, and their sulfation pathways are relatively unexplored. Sulfated polysaccharides possess anti-inflammatory, anticoagulant and anti-cancer properties and have great therapeutic potential. Current identification of PSTs using Pfam has been predominantly focused on the identification of glycosaminoglycan (GAG) sulfotransferases because of their pivotal roles in cell communication, extracellular matrix formation and coagulation. As a result, our knowledge of non-GAG PSTs structure and function remains limited. The major sulfotransferase families, Sulfotransfer_1 and Sulfotransfer_2, display broad homology and should enable the capture of a wide assortment of sulfotransferases but are limited in non-GAG PST sequence annotation. In addition, sequence annotation is further restricted by the paucity of biochemical analyses of PSTs. There are now high-throughput and robust assays for sulfotransferases such as colorimetric PAPS (3′-phosphoadenosine 5′-phosphosulfate) coupled assays, Europium-based fluorescent probes for ratiometric PAP (3′-phosphoadenosine-5′-phosphate) detection, and NMR methods for activity and product analysis. These techniques provide real-time and direct measurements to enhance the functional annotation and subsequent analysis of sulfated polysaccharides across the tree of life to improve putative PST identification and characterisation of function. Improved annotation and biochemical analysis of PST sequences will enhance the utility of PSTs across biomedical and biotechnological sectors.

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Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes

Alempic,

Bisio,

Villalta

et al. 2024

microLife

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The mimivirus 1.2Mb genome was shown to be organized into a nucleocapsid-like genomic fiber encased in the nucleoid compartment inside the icosahedral capsid (Villalta et al. 2022). The genomic fiber protein shell is composed of a mixture of two GMC-oxidoreductase paralogs, one of them being the main component of the glycosylated layer of fibrils at the surface of the virion (Rodrigues et al. 2015). In this study, we determined the effect of the deletion of each of the corresponding genes on the genomic fiber and the layer of surface fibrils. First, we deleted the GMC-oxidoreductase the most abundant in the genomic fiber, and determined its structure and composition in the mutant. As expected, it was composed of the second GMC-oxidoreductase and contained 5- and 6-start helices similar to the wild-type fiber. This result led us to propose a model explaining their coexistence. Then, we deleted the GMC-oxidoreductase the most abundant in the layer of fibrils to analyze its protein composition in the mutant. Second, we showed that the fitness of single mutants and the double mutant were not decreased compared to the wild-type viruses in laboratory conditions. Third, we determined that deleting the GMC-oxidoreductase genes did not impact the glycosylation or the glycan composition of the layer of surface fibrils, despite modifying their protein composition. Since the glycosylation machinery and glycan composition of members of different clades are different (Notaro et al. 2021, Notaro et al. 2022), we expanded the analysis of the protein composition of the layer of fibrils to members of the B and C clades and showed that it was different among the three clades and even among isolates within the same clade. Taken together, the results obtained on two distinct central processes (genome packaging and virion coating) illustrate an unexpected functional redundancy in members of the family Mimiviridae, suggesting this may be the major evolutionary force behind their giant genomes.

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Giant viruses of theMegavirinaesubfamily possess biosynthetic pathways to produce rare bacterial-like sugars in a clade-specific manner

Cited by 11 publications

References 71 publications

The Astounding World of Glycans from Giant Viruses

The Astounding World of Glycans from Giant Viruses

Polysaccharide sulfotransferases: the identification of putative sequences and respective functional characterisation

Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes

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