6BWX

Atomic resolution structure of human bufavirus 1

This is a non-PDB format compatible entry.

Summary for 6BWX

• Entry DOI: 10.2210/pdb6bwx/pdb
• EMDB information: 7300 7301 7302
• Descriptor: VP2 (1 entity in total)
• Functional Keywords: parvovirus, protoparvovirus, virus like particle
• Biological source: Bufavirus-1
• Total number of polymer chains: 60
• Total formula weight: 3694077.18

Authors

Mietzsch, M.,Agbandje-McKenna, M. (deposition date: 2017-12-15, release date: 2018-01-24, Last modification date: 2024-03-13)

Primary citation

Ilyas, M.,Mietzsch, M.,Kailasan, S.,Vaisanen, E.,Luo, M.,Chipman, P.,Smith, J.K.,Kurian, J.,Sousa, D.,McKenna, R.,Soderlund-Venermo, M.,Agbandje-McKenna, M.
Atomic Resolution Structures of Human Bufaviruses Determined by Cryo-Electron Microscopy.
Viruses, 10:-, 2018

PubMed Abstract: Bufavirus strain 1 (BuV1), a member of the genus of the , was first isolated from fecal samples of children with acute diarrhea in Burkina Faso. Since this initial discovery, BuVs have been isolated in several countries, including Finland, the Netherlands, and Bhutan, in pediatric patients exhibiting similar symptoms. Towards their characterization, the structures of virus-like particles of BuV1, BuV2, and BuV3, the current known genotypes, have been determined by cryo-electron microscopy and image reconstruction to 2.84, 3.79, and 3.25 Å, respectively. The BuVs, 65-73% identical in amino acid sequence, conserve the major viral protein, VP2, structure and general capsid surface features of parvoviruses. These include a core β-barrel (βB-βI), α-helix A, and large surface loops inserted between these elements in VP2. The capsid contains depressions at the icosahedral 2-fold and around the 5-fold axes, and has three separated protrusions surrounding the 3-fold axes. Structure comparison among the BuVs and to available parvovirus structures revealed capsid surface variations and capsid 3-fold protrusions that depart from the single pinwheel arrangement of the animal protoparvoviruses. These structures provide a platform to begin the molecular characterization of these potentially pathogenic viruses.

PubMed: 29300333
DOI: 10.3390/v10010022

Experimental method

ELECTRON MICROSCOPY (2.84 Å)