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Cited by 218Animal Virus Infections StudiesParvovirus B19 Infection StudiesEnzyme Structure and Function

Functional implications of the structure of the murine parvovirus, minute virus of mice

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Agbandje-McKenna, Mavis, Llamas-Saiz, Antonio L, Wang, Feng, Tattersall, Peter, Rossmann, Michael G·1998·Structure
DOI 10.1016/s0969-2126(98)00137-3
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Abstract

BACKGROUND: Minute virus of mice (MVM) is a single-stranded (ss) DNA-containing, murine parvovirus with a capsid built up of 60 icosahedrally related polypeptide chains, each of which consists of the C-terminal region common to two structural proteins, VP1 and VP2. In infectious virions, most VP2 molecules are cleaved to VP3 by the removal of about 20 amino acids from the N terminus. Of the 587 amino acids in VP2, approximately half are identical to those in the analogous capsid protein of the antigenically distinct canine parvovirus (CPV), the crystal structure of which has previously been determined. The three-dimensional structure determination of MVMi (the immunosuppressive strain of MVM) was previously reported to 3.5 A resolution. RESULTS: We report here an analysis of the MVMi virus structure and provide insights into tissue tropism, antigenicity and DNA packaging. Amino acids determining MVM tissue tropism were found to cluster on, or near, the viral surface. A conserved, glycine-rich, N-terminal peptide was seen to run through a cylindrical channel along each fivefold axis and may have implications for antigenicity. Density within the virion was interpreted as 29 ssDNA nucleotides per icosahedral asymmetric unit, and accounts for over one-third of the viral genome. CONCLUSIONS: The presence of the glycine-rich sequence in the fivefold channels of MVMi provides a possible mechanism to explain how the unique N-terminal region of VP1 becomes externalized in infectious parvovirions. Residues that determine tropism may form an attachment recognition site for a secondary host-cell factor that modulates tissue specificity. The ordering of nucleotides in a similar region of the interior surface in the CPV and MVMi capsids suggests the existence of a genomic DNA-recognition site within the parvoviral capsid.

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  • Ordered DNA structure has been identified in crystal structures for canine parvovirus and MVM, illustrating that the genome is bound to the interior of the capsid by a specific nucleotide-capsid interaction.

    “It is important to note that ordered DNA structure has been identified in crystal structures for canine parvovirus (CPV) and MVM, illustrating that the genome is bound to the interior of the capsid by a specific nucleotide-capsid interaction (1, 7, 47, 49).”

    From Packaging Capacity of Adeno-Associated Virus Serotypes: Impact of Larger Genomes on Infectivity and Postentry Steps (2005) · cites this paper as [1]

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Cited by

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Authors
Agbandje-McKenna, M., Llamas-Saiz, A. L., Wang, F., Tattersall, P., & Rossmann, M. G.
Affiliations
  • Consejo Superior de Investigaciones Científicas (ES)
  • Yale University (US)
  • Purdue University West Lafayette (US)
Corresponding author
Rossmann, Michael G
ORCID
Venue
Structure
Publisher
Elsevier BV
Published
1998-11
Volume
6
Issue
11
Pages
1369-1381
ISSN
0969-2126 (ISSN-L)
DOI
10.1016/s0969-2126(98)00137-3
OpenAlex
W2035411770
Cited by
218
References
0
Citations by year
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FWCI
10.86
Type
journal article
Language
en
Open access
Licence
Locations
  • Structure (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
Funders
  • Purdue University
  • National Cancer Institute (CA-29303, R01CA029303)
  • National Institute of Allergy and Infectious Diseases (AI11219)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
  • Health Sciences › Medicine › Infectious Diseases › Parvovirus B19 Infection Studies
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
minute virus of mice, parvovirus, capsid structure, VP1, VP2, VP3, tissue tropism, antigenicity, DNA packaging, single-stranded DNA, fivefold symmetry, glycine-rich peptides, canine parvovirus, host cell attachment
MeSH terms
Amino Acid Sequence, Capsid, Glycine, Minute Virus of Mice, Molecular Sequence Data, Protein Conformation, Sequence Homology, Amino Acid, Tropism, Capsid Proteins

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