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8EP2

The capsid structure of Aleutian Mink Disease Virus

This is a non-PDB format compatible entry.
Summary for 8EP2
Entry DOI10.2210/pdb8ep2/pdb
EMDB information28514 28515
DescriptorCapsid protein VP1 (1 entity in total)
Functional Keywordsparvovirus; capsid; amdv; cryo-em; amdoparvovirus; pathogen, virus like particle
Biological sourceAleutian mink disease virus
Total number of polymer chains60
Total formula weight4415718.30
Authors
Mietzsch, M.,McKenna, R. (deposition date: 2022-10-04, release date: 2022-11-09, Last modification date: 2025-05-21)
Primary citationLakshmanan, R.,Mietzsch, M.,Jimenez Ybargollin, A.,Chipman, P.,Fu, X.,Qiu, J.,Soderlund-Venermo, M.,McKenna, R.
Capsid Structure of Aleutian Mink Disease Virus and Human Parvovirus 4: New Faces in the Parvovirus Family Portrait.
Viruses, 14:-, 2022
Cited by
PubMed Abstract: Parvoviruses are small, single-stranded DNA viruses with non-enveloped capsids. Determining the capsid structures provides a framework for annotating regions important to the viral life cycle. Aleutian mink disease virus (AMDV), a pathogen in minks, and human parvovirus 4 (PARV4), infecting humans, are parvoviruses belonging to the genera and , respectively. While Aleutian mink disease caused by AMDV is a major threat to mink farming, no clear clinical manifestations have been established following infection with PARV4 in humans. Here, the capsid structures of AMDV and PARV4 were determined via cryo-electron microscopy at 2.37 and 3.12 Å resolutions, respectively. Despite low amino acid sequence identities (10-30%) both viruses share the icosahedral nature of parvovirus capsids, with 60 viral proteins (VPs) assembling the capsid via two-, three-, and five-fold symmetry VP-related interactions, but display major structural variabilities in the surface loops when the capsid structures are superposed onto other parvoviruses. The capsid structures of AMDV and PARV4 will add to current knowledge of the structural platform for parvoviruses and permit future functional annotation of these viruses, which will help in understanding their infection mechanisms at a molecular level for the development of diagnostics and therapeutics.
PubMed: 36298773
DOI: 10.3390/v14102219
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.37 Å)
Structure validation

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