6HKU

Trichodysplasia spinulosa-associated polyomavirus (TSPyV) VP1 in complex with sialylated precision glycooligomers

Summary for 6HKU

• Entry DOI: 10.2210/pdb6hku/pdb
• Related PRD ID: PRD_900025
• Descriptor: Capsid protein VP1, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: sialic acid derivative, viral protein
• Biological source: Trichodysplasia spinulosa-associated polyomavirus
• Total number of polymer chains: 10
• Total formula weight: 305384.62

Authors

Rustmeier, N.H.,Stehle, T. (deposition date: 2018-09-08, release date: 2019-03-27, Last modification date: 2024-01-17)

Primary citation

Baier, M.,Rustmeier, N.H.,Harr, J.,Cyrus, N.,Reiss, G.J.,Grafmuller, A.,Blaum, B.S.,Stehle, T.,Hartmann, L.
Divalent Sialylated Precision Glycooligomers Binding to Polyomaviruses and the Effect of Different Linkers.
Macromol Biosci, 19:e1800426-e1800426, 2019

PubMed Abstract: Divalent precision glycooligomers terminating in N-acetylneuraminic acid (Neu5Ac) or 3'-sialyllactose (3'-SL) with varying linkers between scaffold and the glycan portions are synthesized via solid phase synthesis for co-crystallization studies with the sialic acid-binding major capsid protein VP1 of human Trichodysplasia spinulosa-associated Polyomavirus. High-resolution crystal structures of complexes demonstrate that the compounds bind to VP1 depending on the favorable combination of carbohydrate ligand and linker. It is found that artificial linkers can replace portions of natural carbohydrate linkers as long as they meet certain requirements such as size or flexibility to optimize contact area between ligand and receptor binding sites. The obtained results will influence the design of future high affinity ligands based on the structures presented here, and they can serve as a blueprint to develop multivalent glycooligomers as inhibitors of viral adhesion.

PubMed: 30884172
DOI: 10.1002/mabi.201800426

Experimental method

X-RAY DIFFRACTION (1.98 Å)