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Virus-encoded movement protein (MP) mediates cell-to-cell spread of tobacco mosaic virus (TMV) through plant intercellular connections, the plasmodesmata. The molecular pathway by which TMV MP interacts with the host cell is largely unknown. To understand this process better, a cell wall-associated protein that specifically binds the viral MP was purified from tobacco leaf cell walls and identified as pectin methylesterase (PME). In addition to TMV MP, PME is recognized by MPs of turnip vein clearing virus (TVCV) and cauliflower mosaic virus (CaMV). The use of amino acid deletion mutants of TMV MP showed that its domain was necessary and sufficient for association with PME. Deletion of the PME-binding region resulted in inactivation of TMV cell-to-cell movement.

Original publication

DOI

10.1093/emboj/19.5.913

Type

Journal article

Journal

EMBO J

Publication Date

01/03/2000

Volume

19

Pages

913 - 920

Keywords

Amino Acid Sequence, Binding Sites, Carboxylic Ester Hydrolases, Molecular Sequence Data, Plant Viral Movement Proteins, Plants, Toxic, Protein Binding, Sequence Alignment, Tobacco, Tobacco Mosaic Virus, Viral Proteins, Virus Replication