A Family of Plasmodesmal Proteins with Receptor-Like Properties for Plant Viral Movement Proteins

PLoS Pathogens

Andrew J. Maule¹  Carole L. Thomas¹  Lourdes Fernandez-Calvino¹  Alexander Lerich²  Jérome Mutterer²  Manfred Heinlein²  Emmanuel Boutant²  Corinne Schmitt-Keichinger²  Christophe Ritzenthaler²  Christina Hofmann²  Khalid Amari²  Yves Mély³  Pascal Didier³ 

[1] Department of Disease and Stress Biology, John Innes Centre, Norwich Research Park, Norwich, United Kingdom;Institut de Biologie Moléculaire des Plantes du CNRS, Université de Strasbourg, Strasbourg, France;UMR 7213 CNRS, Biophotonique et Pharmacologie/Université de Strasbourg, Faculté de Pharmacie, Illkirch, France

关键词: Arabidopsis thaliana;    Fluorescence imaging;    Membrane proteins;    Leaves;    Fluorescence resonance energy transfer;    Endoplasmic reticulum;    Cell membranes;    Plasmodesmata;   

DOI  :  10.1371/journal.ppat.1001119

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

Plasmodesmata (PD) are essential but poorly understood structures in plant cell walls that provide symplastic continuity and intercellular communication pathways between adjacent cells and thus play fundamental roles in development and pathogenesis. Viruses encode movement proteins (MPs) that modify these tightly regulated pores to facilitate their spread from cell to cell. The most striking of these modifications is observed for groups of viruses whose MPs form tubules that assemble in PDs and through which virions are transported to neighbouring cells. The nature of the molecular interactions between viral MPs and PD components and their role in viral movement has remained essentially unknown. Here, we show that the family of PD-located proteins (PDLPs) promotes the movement of viruses that use tubule-guided movement by interacting redundantly with tubule-forming MPs within PDs. Genetic disruption of this interaction leads to reduced tubule formation, delayed infection and attenuated symptoms. Our results implicate PDLPs as PD proteins with receptor-like properties involved the assembly of viral MPs into tubules to promote viral movement.

【 授权许可】

CC BY