You are here

Atomic Resolution Structures Of Human Bufaviruses Determined By Cryo-electron Microscopy

Title: Atomic Resolution Structures Of Human Bufaviruses Determined By Cryo-electron Microscopy.
7 views
1 downloads
Name(s): Ilyas, Maria, author
Mietzsch, Mario, author
Kailasan, Shweta, author
Vaisanen, Elina, author
Luo, Mengxiao, author
Chipman, Paul, author
Smith, J. Kennon, author
Kurian, Justin, author
Sousa, Duncan, author
McKenna, Robert, author
Soderlund-Venermo, Maria, author
Agbandje-McKenna, Mavis, author
Type of Resource: text
Genre: Journal Article
Text
Journal Article
Date Issued: 2018-01
Physical Form: computer
online resource
Extent: 1 online resource
Language(s): English
Abstract/Description: Bufavirus strain 1 (BuV1), a member of the Protoparvovirus genus of the Parvoviridae, 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 angstrom, 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 -barrel (B-I), -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.
Identifier: FSU_libsubv1_wos_000424414900022 (IID), 10.3390/v10010022 (DOI)
Keywords: complex, adenoassociated virus-2, bufavirus, cellular receptor, cryo-EM and image reconstruction, diarrhea, electron-microscopy, empty capsids, human parvovirus b19, human protoparvoviruses, parvoviruses, porcine parvovirus, single-stranded DNA virus, surface loops
Publication Note: The publisher's version of record is available at https://doi.org/10.3390/v10010022
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_libsubv1_wos_000424414900022
Host Institution: FSU
Is Part Of: Viruses-Basel.
1999-4915
Issue: iss. 1, vol. 10

Choose the citation style.
Ilyas, M., Mietzsch, M., Kailasan, S., Vaisanen, E., Luo, M., Chipman, P., … Agbandje-McKenna, M. (2018). Atomic Resolution Structures Of Human Bufaviruses Determined By Cryo-electron Microscopy. Viruses-Basel. Retrieved from http://purl.flvc.org/fsu/fd/FSU_libsubv1_wos_000424414900022