Polerovirus N-terminal readthrough domain structures reveal molecular strategies for mitigating virus transmission by aphids

Journal Article · Wed Oct 26 00:00:00 EDT 2022 · Nature Communications

DOI:https://doi.org/10.1038/s41467-022-33979-2· OSTI ID:1894717

Schiltz, Carl J. ; Wilson, Jennifer R. ; Hosford, Christopher J.; Adams, Myfanwy C.; Preising, Stephanie E.; DeBlasio, Stacy L.; MacLeod, Hannah J.; Van Eck, Joyce; Heck, Michelle L. ; Chappie, Joshua S.

Abstract Poleroviruses, enamoviruses, and luteoviruses are icosahedral, positive sense RNA viruses that cause economically important diseases in food and fiber crops. They are transmitted by phloem-feeding aphids in a circulative manner that involves the movement across and within insect tissues. The N-terminal portion of the viral readthrough domain ( ^N RTD) has been implicated as a key determinant of aphid transmission in each of these genera. Here, we report crystal structures of the ^N RTDs from the poleroviruses turnip yellow virus (TuYV) and potato leafroll virus (PLRV) at 1.53-Å and 2.22-Å resolution, respectively. These adopt a two-domain arrangement with a unique interdigitated topology and form highly conserved dimers that are stabilized by a C-terminal peptide that is critical for proper folding. We demonstrate that the PLRV ^N RTD can act as an inhibitor of virus transmission and identify ^N RTD mutant variants that are lethal to aphids. Sequence conservation argues that enamovirus and luteovirus ^N RTDs will follow the same structural blueprint, which affords a biological approach to block the spread of these agricultural pathogens in a generalizable manner.

• Sponsoring Organization: USDOE
• Grant/Contract Number: AC02-06CH11357
• OSTI ID: 1894717
• Journal Information: Nature Communications, Journal Name: Nature Communications Vol. 13 Journal Issue: 1; ISSN 2041-1723
• Publisher: Nature Publishing Group
• Country of Publication: United Kingdom
• Language: English