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Chloroplast Fibrillin-Mediated α-Tocopherol Biosynthesis Impaired by a Virus to Enhance Infection and to Improve
Sijia Liu1,2, Xuedong Liu1,3, Qin Yan1
1State Key Laboratory of Agricultural and Forestry Biosecurity, Key Laboratory of Surveillance and Management for Plant Quarantine Pests, Ministry of Agriculture and Rural Affairs, P. R. China, Department of Plant Pathology, China Agricultural University, Beijing, 100193, China.
Abstract:
Plastoglobules (PGs), the lipid droplets mainly within chloroplasts, are crucial for plant redox homeostasis and environmental adaptation. However, the regulation of PG under stress remains elusive. This study uncovers that PGs are targeted by the p22 protein encoded by an emerging virus-tomato chlorosis virus (ToCV), leading to impaired α-tocopherol biosynthesis, thereby facilitating viral infection and improving drought resistance. Specially, ToCV-encoded p22 protein co-opts the PG structural protein fibrillin (FBN) to access PG, where it impairs α-tocopherol biosynthesis via disturbing the interaction between FBN1.1 and tocopherol cyclase (VTE1). Alpha-tocopherol is required for both preventing lipid peroxidation in the thylakoid membrane and suppressing ToCV infection. Infection of ToCV or transgenic expression of p22 protein inhibits α-tocopherol biosynthesis, resulting in chloroplast oxidative stress, which may contribute to the accumulation of 3'-phosphoadenosine 5'-phosphate (PAP), a retrograde signal from chloroplasts to the nucleus that triggers drought tolerance. Taken together, FBN1.1 modulates plant-virus-drought interaction via regulating the function of PG.
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