The cysteine residues at the C-terminal tail of Bamboo mosaic virus triple gene block protein 2 are critical for efficient plasmodesmata localization of protein 1 in the same block

• Published in: Virology (New York, N.Y.) Vol. 501; pp. 47 - 53
• Main Authors: Ho, Tsai-Ling, Lee, Hsiang-Chi, Chou, Yuan-Lin, Tseng, Yang-Hao, Huang, Wei-Cheng, Wung, Chiung-Hua, Lin, Na-Sheng, Hsu, Yau-Heiu, Chang, Ban-Yang
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.01.2017
• Subjects: Amino Acid Motifs; Bamboo mosaic virus; Cell-to-cell movement; Cysteine - genetics; Cysteine - metabolism; Infectious Disease; Nicotiana - virology; Plant Diseases - virology; Plasmodesmata - metabolism; Plasmodesmata - virology; Plasmodesmata targeting; Potexvirus - chemistry; Potexvirus - genetics; Potexvirus - metabolism; Protein Transport; Triple gene block proteins; Viral Proteins - chemistry; Viral Proteins - genetics; Viral Proteins - metabolism; Plasmodesmata targeting; Triple gene block proteins; Cell-to-cell movement; Bamboo mosaic virus
• ISSN: 0042-6822; 1096-0341
• DOI: 10.1016/j.virol.2016.11.005

Abstract The movement of some plant viruses are accomplished by three proteins encoded by a triple gene block (TGB). The second protein (TGBp2) in the block is a transmembrane protein. This study was aimed to unravel the mechanism underlying the relatively inefficient cell-to-cell movement of Bamboo mosaic virus (BaMV) caused by amino acid substitutions for the three Cys residues, Cys-109, Cys-112 and Cys-119, at the C-terminal tail of TGBp2. Results from confocal microscopy revealed that substitutions of the three Cys residues of TGBp2, especially Cys-109 and Cys-112, would reduce the efficiency of TGBp2- and TGBp3-dependent PD localization of TGBp1. Moreover, there is an additive effect of the substitutions on reducing the efficiency of PD localization of TGBp1. These results indicate that the Cys residues in the C-terminal tail region of TGBp2 participate in the TGBp2- and TGBp3-dependent PD localization of TGBp1, and thus influence the cell-to-cell movement capability of BaMV.