Unknown

Dataset Information

0

Twenty-Five Years of Structural Parvovirology.


ABSTRACT: Parvoviruses, infecting vertebrates and invertebrates, are a family of single-stranded DNA viruses with small, non-enveloped capsids with T = 1 icosahedral symmetry. A quarter of a century after the first parvovirus capsid structure was published, approximately 100 additional structures have been analyzed. This first structure was that of Canine Parvovirus, and it initiated the practice of structure-to-function correlation for the family. Despite high diversity in the capsid viral protein (VP) sequence, the structural topologies of all parvoviral capsids are conserved. However, surface loops inserted between the core secondary structure elements vary in conformation that enables the assembly of unique capsid surface morphologies within individual genera. These variations enable each virus to establish host niches by allowing host receptor attachment, specific tissue tropism, and antigenic diversity. This review focuses on the diversity among the parvoviruses with respect to the transcriptional strategy of the encoded VPs, the advances in capsid structure-function annotation, and therapeutic developments facilitated by the available structures.

SUBMITTER: Mietzsch M 

PROVIDER: S-EPMC6521121 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

altmetric image

Publications

<b>Twenty-Five Years of Structural Parvovirology</b>.

Mietzsch Mario M   Pénzes Judit J JJ   Agbandje-McKenna Mavis M  

Viruses 20190420 4


Parvoviruses, infecting vertebrates and invertebrates, are a family of single-stranded DNA viruses with small, non-enveloped capsids with T = 1 icosahedral symmetry. A quarter of a century after the first parvovirus capsid structure was published, approximately 100 additional structures have been analyzed. This first structure was that of Canine Parvovirus, and it initiated the practice of structure-to-function correlation for the family. Despite high diversity in the capsid viral protein (VP) s  ...[more]

Similar Datasets

| S-EPMC8654240 | biostudies-literature
| S-EPMC6393861 | biostudies-literature
| S-EPMC6680191 | biostudies-literature
| S-EPMC9498654 | biostudies-literature
| S-EPMC5531806 | biostudies-other
| S-EPMC5692607 | biostudies-literature
| S-EPMC6838951 | biostudies-literature
| S-EPMC7089755 | biostudies-literature
| S-EPMC18144 | biostudies-literature
| S-EPMC3739974 | biostudies-literature