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

Carl J. Schiltz, Jennifer R. Wilson, Christopher J. Hosford, Myfanwy C. Adams, Stephanie E. Preising, Stacy L. DeBlasio, Hannah J. MacLeod, Joyce Van Eck, Michelle L. Heck () and Joshua S. Chappie ()
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Carl J. Schiltz: Cornell University
Jennifer R. Wilson: Cornell University
Christopher J. Hosford: Cornell University
Myfanwy C. Adams: Cornell University
Stephanie E. Preising: Cornell University
Stacy L. DeBlasio: Cornell University
Hannah J. MacLeod: Emerging Pest and Pathogen Research Unit
Joyce Van Eck: Cornell University
Michelle L. Heck: Cornell University
Joshua S. Chappie: Cornell University

Nature Communications, 2022, vol. 13, issue 1, 1-13

Abstract: 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 (NRTD) has been implicated as a key determinant of aphid transmission in each of these genera. Here, we report crystal structures of the NRTDs 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 NRTD can act as an inhibitor of virus transmission and identify NRTD mutant variants that are lethal to aphids. Sequence conservation argues that enamovirus and luteovirus NRTDs will follow the same structural blueprint, which affords a biological approach to block the spread of these agricultural pathogens in a generalizable manner.

Date: 2022
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DOI: 10.1038/s41467-022-33979-2

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