Anno2013
AutoriFederica Martellini (1); Franco Faoro (2); Lara Carresi (39; Barbara Pantera (1); Ivan Baccelli (3); Dario Maffi (2); Bruno Tiribilli (4); Francesca Sbrana (5); Simone Luti (1); Cecilia Comparini (3); Rodolfo Bernardi (6); Gianni Cappugi (1); Aniello Scal
AbstractBased on sequence homology, several fungal Cys-rich secreted proteins have been grouped in the cerato-platanin (CP) family, which comprises at least 40 proteins involved mainly in eliciting defense-related responses. The core member of this family is cerato-platanin, a moderately hydrophobic protein with a double ?-? barrel fold. CP and the recently identified orthologous cerato-populin (Pop1) are involved in host-fungus interaction, and can be considered non-catalytic fungal PAMPs. CP is more active in inducing defense when in an aggregated conformation than in its native form, but little is known about other CP-orthologous proteins. Here, we cloned, expressed, and purified recombinant Pop1, which was used to characterize the protein aggregates. Our results suggest that the unfolded, self-assembled Pop1 is more active in inducing defense, and that the unfolding process can be induced by interaction with hydrophobic inanimate surfaces such as Teflon, treated mica, and gold sheets. In vivo, we found that both CP and Pop1 interact with the hydrophobic cuticle of leaves. Therefore, we propose that the interaction of these proteins with host cuticle waxes could induce unfolding and consequently trigger their PAMP-like activity.
RivistaMolecular Biotechnology
ISSN1073-6085
Impact factor
Volume55
Pagina inizio27
Pagina fine42
Autori IBFFrancesca SBRANA
Linee di Ricerca IBFMD.P01.001.001
Sedi IBFIBF.GE