English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Significance Parvoviruses (PVs) are ssDNA viruses, with T = 1 icosahedral symmetry, infecting deuterostome and protostome animals. Most PVs have a highly conserved phospholipase A2 domain (PLA2) in the N-terminal region of their minor capsid protein. Under acidic pH, during endosomal/lysosomal egress, the PLA2 domain is activated to disrupt vesicle membranes. However, certain PVs lack the PLA2 and thus must use a different escape mechanism. Our study offers insight into this enigma, showing how a recently discovered PV of marine crustacean has evolved a cation-dependent mechanism to accomplish this task. We also show how host-driven convergent evolution pushed two PVs, infecting the same host species, to adopt strikingly similar surface morphologies, despite distinct multimer interactions and lack of sequence similarity.

Molecular biology and structure of a novel penaeid shrimp densovirus elucidate convergent parvoviral host capsid evolution