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4POT

Structure of Human Polyomavirus 9 VP1 pentamer in complex with N-glycolylneuraminic acid containing 3'-sialyllactosamine

Summary for 4POT
Entry DOI10.2210/pdb4pot/pdb
Related4FMI 4MBZ 4POQ 4POR 4POS
DescriptorVP1, N-glycolyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (6 entities in total)
Functional Keywordsjelly roll fold, capsid formation, receptor interaction, carbohydrate, sialyloligosaccharide, viral coat protein, viral protein
Biological sourceHuman polyomavirus 9
Total number of polymer chains10
Total formula weight311287.50
Authors
Khan, Z.M.,Stehle, T. (deposition date: 2014-02-26, release date: 2014-04-09, Last modification date: 2024-11-06)
Primary citationKhan, Z.M.,Liu, Y.,Neu, U.,Gilbert, M.,Ehlers, B.,Feizi, T.,Stehle, T.
Crystallographic and glycan microarray analysis of human polyomavirus 9 VP1 identifies N-glycolyl neuraminic acid as a receptor candidate.
J.Virol., 88:6100-6111, 2014
Cited by
PubMed Abstract: Human polyomavirus 9 (HPyV9) is a closely related homologue of simian B-lymphotropic polyomavirus (LPyV). In order to define the architecture and receptor binding properties of HPyV9, we solved high-resolution crystal structures of its major capsid protein, VP1, in complex with three putative oligosaccharide receptors identified by glycan microarray screening. Comparison of the properties of HPyV9 VP1 with the known structure and glycan-binding properties of LPyV VP1 revealed that both viruses engage short sialylated oligosaccharides, but small yet important differences in specificity were detected. Surprisingly, HPyV9 VP1 preferentially binds sialyllactosamine compounds terminating in 5-N-glycolyl neuraminic acid (Neu5Gc) over those terminating in 5-N-acetyl neuraminic acid (Neu5Ac), whereas LPyV does not exhibit such a preference. The structural analysis demonstrated that HPyV9 makes specific contacts, via hydrogen bonds, with the extra hydroxyl group present in Neu5Gc. An equivalent hydrogen bond cannot be formed by LPyV VP1.
PubMed: 24648448
DOI: 10.1128/JVI.03455-13
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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數據於2024-11-06公開中

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