8AH1

BK Polyomavirus VP1 mutant N-Q

This is a non-PDB format compatible entry.

Summary for 8AH1

• Entry DOI: 10.2210/pdb8ah1/pdb
• Related: 8AGH 8AGO 8AH0
• Descriptor: Major capsid protein VP1, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: patient-derived vp1 mutant, viral protein
• Biological source: Betapolyomavirus hominis
• Total number of polymer chains: 10
• Total formula weight: 299129.63

Authors

Sorin, M.N.,Di Maio, A.,Silva, L.M.,Ebert, D.,Delannoy, C.,Nguyen, N.-K.,Guerardel, Y.,Chai, W.,Halary, F.,Renaudin-Autain, K.,Liu, Y.,Bressollette-Bodin, C.,Stehle, T.,McIlroy, D. (deposition date: 2022-07-20, release date: 2023-02-22, Last modification date: 2024-02-07)

Primary citation

Sorin, M.N.,Di Maio, A.,Silva, L.M.,Ebert, D.,Delannoy, C.P.,Nguyen, N.K.,Guerardel, Y.,Chai, W.,Halary, F.,Renaudin-Autain, K.,Liu, Y.,Bressollette-Bodin, C.,Stehle, T.,McIlroy, D.
Structural and functional analysis of natural capsid variants suggests sialic acid-independent entry of BK polyomavirus.
Cell Rep, 42:112114-112114, 2023

PubMed Abstract: BK polyomavirus (BKPyV) is an opportunistic pathogen that uses the b-series gangliosides GD1b and GT1b as entry receptors. Here, we characterize the impact of naturally occurring VP1 mutations on ganglioside binding, VP1 protein structure, and virus tropism. Infectious entry of single mutants E73Q and E73A and the triple mutant A72V-E73Q-E82Q (VQQ) remains sialic acid dependent, and all three variants acquire binding to a-series gangliosides, including GD1a. However, the E73A and VQQ variants lose the ability to infect ganglioside-complemented cells, and this correlates with a clear shift of the BC2 loop in the crystal structures of E73A and VQQ. On the other hand, the K69N mutation in the K69N-E82Q variant leads to a steric clash that precludes sialic acid binding. Nevertheless, this mutant retains significant infectivity in 293TT cells, which is not dependent on heparan sulfate proteoglycans, implying that an unknown sialic acid-independent entry receptor for BKPyV exists.

PubMed: 36790933
DOI: 10.1016/j.celrep.2023.112114

Experimental method

X-RAY DIFFRACTION (2.006 Å)