Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid

Suriyasri Subramanian, Lindsey J. Organtini, Alec Grossman, Phillip P. Domeier, Javier O. Cifuente, Alexander M. Makhov, James F. Conway, Anthony D'Abramo, Susan F. Cotmore, Peter Tattersall, Susan Hafenstein

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4 Scopus citations

Abstract

In minute virus of mice (MVM) capsids, icosahedral five-fold channels serve as portals mediating genome packaging, genome release, and the phased extrusion of viral peptides. Previous studies suggest that residues L172 and V40 are essential for channel function. The structures of MVMi wildtype, and mutant L172T and V40A virus-like particles (VLPs) were solved from cryo-EM data. Two constriction points, termed the mid-gate and inner-gate, were observed in the channels of wildtype particles, involving residues L172 and V40 respectively. While the mid-gate of V40A VLPs appeared normal, in L172T adjacent channel walls were altered, and in both mutants there was major disruption of the inner-gate, demonstrating that direct L172:V40 bonding is essential for its structural integrity. In wildtype particles, residues from the N-termini of VP2 map into claw-like densities positioned below the channel opening, which become disordered in the mutants, implicating both L172 and V40 in the organization of VP2 N-termini.

Original languageEnglish (US)
Pages (from-to)216-223
Number of pages8
JournalVirology
Volume510
DOIs
StatePublished - Oct 2017

All Science Journal Classification (ASJC) codes

  • Virology

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    Subramanian, S., Organtini, L. J., Grossman, A., Domeier, P. P., Cifuente, J. O., Makhov, A. M., Conway, J. F., D'Abramo, A., Cotmore, S. F., Tattersall, P., & Hafenstein, S. (2017). Cryo-EM maps reveal five-fold channel structures and their modification by gatekeeper mutations in the parvovirus minute virus of mice (MVM) capsid. Virology, 510, 216-223. https://doi.org/10.1016/j.virol.2017.07.015