16 research outputs found
Caractérisation d'anticorps dirigés contre la VPg du virus de la mosaïque de la laitue (LMV)
National audienc
Introduction of a NIa proteinase cleavage site between the reporter gene and HC-Pro only partially restores the biological properties of GUS- or GFP-tagged LMV
Interaction between potyvirus helper component-proteinase and capsid protein in infected plants
Monoclonal antibodies were raised against helper component-proteinase (HcPro) purified from plants infected with the potyvirus Lettuce mosaic virus (LMV). These antibodies were used in a two-site triple antibody sandwich ELISA assay together with polyclonal antibodies directed against purified virions. An interaction between HcPro and the viral coat protein (CP) was demonstrated in extracts of LMV-infected leaves, as well as for two other potyviruses, Plum pox virus and Potato virus Y. The CP–HcPro interaction was not abolished in LMV derivatives with an HcPro GFP N-terminal fusion, or with a deletion from the CP of the amino acids involved in aphid transmission. Electron microscopy indicated that HcPro probably does not interact with the CP in the form of assembled virions or virus-like particles. Together, these results suggest that the interaction detected between CP and HcPro might be involved in a process of the potyvirus cycle different from aphid transmission
Resistance mechanism against LMV in lettuce involving eIF4E, VPg and CI: beyond the tip of the iceberg
Redox-Immunofunctionalized Potyvirus Nanoparticles for High-Resolution Imaging by AFM-SECM Correlative Microscopy.
We present in this chapter a new experimental approach allowing the high resolution imaging of immune complexes on virus particles. Combined atomic force-electrochemical microscopy (AFM-SECM) is used to image the presence of ferrocene functionalized specific antibodies on the surface of potyvirus particles. For this purpose, potyviruses, flexuous filamentous phytoviruses with a high aspect ratio, have been chosen. This technique allows analysis of the distribution of antibody labeling over the virus population. But, more importantly, it opens up the imaging of immune complexes decorating a single viral particle. Finally, its high resolution allows the characterization in situ of the ultrastructure of a single immune complex on the particle