6533b871fe1ef96bd12d2402
RESEARCH PRODUCT
Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein
Antonio CruzLuis Martínez-gilIsmael MingarroVicente PallásJesús Pérez-gilJesús A. Sánchez-navarrosubject
ImmunologyMolecular Sequence DataMicrobiologiaBiologyIlarvirusMicrobiologyCell membraneSequence Analysis ProteinVirologymedicineAmino Acid SequenceMovement proteinPeptide sequenceIntegral membrane proteinPhospholipidsEndoplasmic reticulumCircular DichroismCell MembraneProteïnes de membranaBiological membraneVirus InternalizationTransmembrane proteinCell biologyVirus-Cell InteractionsVirusPlant Viral Movement ProteinsMembranemedicine.anatomical_structureBiochemistryInsect ScienceMutationPrunusHydrophobic and Hydrophilic InteractionsSequence Alignmentdescription
ABSTRACT The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline residue located in the middle of the HR constrains the structural conformation of this region at the membrane interface, and its replacement precludes virus movement.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2009-01-01 |