MAP30 and luffin-α: Novel ribosome-inactivating proteins induce plant systemic resistance against plant viruses

Abstract

Ribosome-inactivating proteins (RIPs) are toxic N-glycosylase that act on eukaryotic and prokaryotic rRNAs, resulting in arrest protein synthesis. RIPs are widely found in higher plant species and display strong antiviral activity. Previous studies have shown that PAP and α-MMC have antiviral activity against TMV. However, the localization of RIPs in plant cells and the mechanism by which RIPs activate plant defense against several plant viruses remain unclear. In this study, we obtained four RIPs (the C-terminal deletion mutant of pokeweed antiviral proteins (PAP-c), alpha-momorcharin (α-MMC), momordica anti-HIV protein of 30 kDa (MAP30) and luffin-α). The subcellular localization results indicated that these four RIPs were located on the plant cell membrane. Heterologous expression of RIPs (PAP-c, α-MMC, MAP30, luffin-α) enhanced tobacco mosaic virus (TMV) resistance in N. benthamiana. Compared with the control treatment, these RIPs significantly reduced the TMV content (149–357 fold) and altered the movement of TMV in the leaves of N. benthamiana. At the same time, heterologous expression of RIPs (MAP30 and luffin-α) could relieve TMV-induced oxidative damage, significantly inducing the expression of plant defense genes including PR1 and PR2. Furthermore, application of these RIPs could inhibit the infection of turnip mosaic virus (TuMV) and potato virus x (PVX). Therefore, this study demonstrated that MAP30 and luffin-α could be considered as new, effective RIPs for controlling plant viruses by activating plant systemic defense.