Interactions between the tomato spotted wilt virus movement protein and plant proteins showing homologies to myosin, kinesin and DnaJ-like chaperones

Capsid Protein-Mediated Recruitment of Host DnaJ-Like Proteins Is Required for Potato Virus Y Infection in Tobacco Plants

“…However, the identified NtCPIPs fall into a distinct subclass that contain only the J domain. Strikingly, the group of DnaJ-like proteins from tobacco (NtDnaJ_M541), tomato (Le19/8) and Arabidopsis (AtA39), which were recently isolated as TSWV MP (NSm)-binding proteins, also lack, except for the common J domain, domain structures typically found in DnaJ (66,70). Instead, motifs for a Lys-rich domain (4x K-X-X-X-K-E/K) were identified that are also partially present in the NtCPIP proteins (aa 172 to 177 and aa 269 to 274 for NtCPIP1 and aa 171 to 176 and aa 168 to 273 for NtCPIP2a and -2b, Fig.…”

“…Due to the presence of a conserved J-domain (44) at the N terminus (aa 4 to 68 for NtCPIP1 and aa 4 to 70 for NtCPIP2a/2b, respectively), the CP-interacting NtCPIPs could be assigned to the large and diverse family of DnaJ-like proteins, and highest similarity was detected to several DnaJlike genes from Arabidopsis thaliana (GenBank accession numbers AAD39315, AAS32885, AAF07844, AAD25656, and T48181). Interestingly, NtCPIPs also shared substantial similarity with a subset of J-domain proteins encoded by the N. tabacum gene NtDnaJ_M541 (59.2% identity on amino acid level) and its Lycopersicon esculentum Le19/8 (59.5%) and Arabidopsis thaliana AtA39 (59.8%) orthologues that were previously identified to interact with the TSWV movement protein NSm (66,70). However, PVY CP was unable to bind NtDnaJ_M541 and consistently TSWV NSm did not interact with the different NtCPIPs in yeast (Fig.…”

“…However, the biological role for most of these unrelated host proteins during virus spread has yet to be elucidated. In addition, screening of a yeast two-hybrid library with the Tomato spotted wilt tospovirus (TSWV) MP (NSm) led to the isolation of a myosin/ kinesin-like protein, as well as DnaJ-like (HSP40) proteins from different plant species, suggesting the involvement of the cytoskeleton and the recruitment of HSP70-related chaperones in TSWV movement (66,70). A direct role of molecular chaperones in virus movement was corroborated by functional analysis of a HSP70 homolog encoded by closteroviruses that was demonstrated to associate with PD and to exhibit distinct functions in virion assembly and cell-to-cell movement (2,51,55).…”

Identification and characterization of host proteins interacting with NSm, the Tomato spotted wilt virus movement protein

“…Therefore, alternative approaches occurred to be the method of choice to eludidate on the role of virus -as well as host proteins during infection. Using the yeast two-hybrid system and far-western analysis, J-domain chaperones and a protein of unknown function aligning to myosins and kinesins, denominated At-4/1, have been identified as interacting partners of the TSWV encoded NSm movement protein (VON BARGEN et al 2001;SOELLICK et al 2000).…”

Reactive oxygen and nitrogen species and hormone signalling in systemic infection of pea by Pea enation mosaic virus

“…These highly conserved proteins are classified into five major families, from which plant Hsp70s contribute substantially to the folding and turnover of viral proteins. Chaperones have been reported to enable virus translocation, and thus the development of the disease, via the interaction with viral movement protein (von Bargen et al 2001). Studies of Chen et al (2008) suggested that cytoplasmic Hsp70 family members play important roles in plant RNA virus multiplication, from gene expression to virion assembly, which enhances the infection degree.…”