AI-driven structural informatics reveals diverse glycosylation machinery across double-stranded DNA viruses
Abstract
Glycosylation is widespread in biology and shapes molecular recognition, yet the diversity and biosynthetic organization of viral glycosyltransferases (GTs) remain poorly understood. Here we integrate structural-alphabet-guided searches and structure similarity networks with genomic-neighbourhood and biosynthetic gene cluster embedding analyses to examine viral GT-A proteins. This approach reveals extensive structural diversity overlooked by sequence-based annotation, including previously uncharacterized viral GT lineages. Most strikingly, we identified a jumbo-phage locus encoding five tandem glycosyltransferases alongside hydroxymethyl-pyrimidine biosynthetic and sulfation-associated enzymes, suggesting a previously unrecognized form of viral DNA modification involving a sulfated pentasaccharide. Beyond these examples, predicted saccharide-associated loci span divergent double-stranded DNA viruses, from giant viruses to tailed phages, and occupy multiple regions of the reference biosynthetic landscape. Together, our findings uncover an underappreciated repertoire of virus-encoded glycosylation machinery and suggest that viral glycan biosynthesis encompasses diverse molecular contexts and potential biological functions.
Related
- Deep Intact Glycoproteomic Analysis Reveals Multi-Level Glycosylation Heterogeneity in Renal Tumors
- Structural dynamics of substrate processing by the p97-Ufd1-Npl4-FAF1 machinery
- STRUCTURAL AND MOLECULAR DYNAMICS ANALYSIS OF HUMAN β-DEFENSIN 1 VARIANTS REVEALS DISTINCT PERTURBATION SIGNATURES
- Structural analysis reveals three families of bacterial tRNA mimics
- Long-read genome assembly of high-erucic-acid Brassica napus reveals candidate structural variants in fatty acid metabolism genes
BibTeX
@misc{na2026aidriven,
title = {{AI-driven structural informatics reveals diverse glycosylation machinery across double-stranded DNA viruses}},
author = {Lan Na},
howpublished = {arXiv},
year = {2026},
month = oct,
doi = {10.48550/arxiv.2610.39662},
eprint = {2610.39662},
archivePrefix = {arXiv},
url = {https://arxiv.org/abs/2610.39662},
note = {CC BY 4.0},
}
RIS
TY - UNPB
TI - AI-driven structural informatics reveals diverse glycosylation machinery across double-stranded DNA viruses
AU - Lan Na
PY - 2026
DA - 2026/10/29
PB - arXiv
DO - 10.48550/arxiv.2610.39662
UR - https://arxiv.org/abs/2610.39662
AB - Glycosylation is widespread in biology and shapes molecular recognition, yet the diversity and biosynthetic organization of viral glycosyltransferases (GTs) remain poorly understood. Here we integrate structural-alphabet-guided searches and structure similarity networks with genomic-neighbourhood and biosynthetic gene cluster embedding analyses to examine viral GT-A proteins. This approach reveals extensive structural diversity overlooked by sequence-based annotation, including previously uncharacterized viral GT lineages. Most strikingly, we identified a jumbo-phage locus encoding five tandem glycosyltransferases alongside hydroxymethyl-pyrimidine biosynthetic and sulfation-associated enzymes, suggesting a previously unrecognized form of viral DNA modification involving a sulfated pentasaccharide. Beyond these examples, predicted saccharide-associated loci span divergent double-stranded DNA viruses, from giant viruses to tailed phages, and occupy multiple regions of the reference biosynthetic landscape. Together, our findings uncover an underappreciated repertoire of virus-encoded glycosylation machinery and suggest that viral glycan biosynthesis encompasses diverse molecular contexts and potential biological functions.
ER -