Plant pathogenic fungi secrete a lot of non-catalytic proteins, which are involved in various aspects of pathogenesis. These proteins are classified in seven fungal protein families, including the cerato-platanin (CP) family (PF07249). Since a single family contains proteins with different functions in the plant pathogenesis, and different families may contain proteins with similar functions, we aimed to investigate why this happens. For this purpose we developed a study model represented by two proteins belonging to the CP family: CP, the founder protein produced by Ceratocystis platani, and the CP-orthologous cerato-populin (Pop1) produced by C. populicola. Both CP and Pop1 have been purified, cloned in P. pastoris, expressed, and characterized for their ability to aggregate. They are well-structured α/β proteins (the 3D-structure of CP has been recently determined), and have only the 70.1% of the amino acids identical or highly conserved. Moreover, they behave as PAMPs, since it stimulated plants to activate defense responses able to reduce consistently the fungal growth. Their capability to elicit differently defense events and their role in fungal physiology is under study.
The cerato-platanins: non-catalytic proteins with functions in the relational life of fungi
BERNARDI, RODOLFO;
2009-01-01
Abstract
Plant pathogenic fungi secrete a lot of non-catalytic proteins, which are involved in various aspects of pathogenesis. These proteins are classified in seven fungal protein families, including the cerato-platanin (CP) family (PF07249). Since a single family contains proteins with different functions in the plant pathogenesis, and different families may contain proteins with similar functions, we aimed to investigate why this happens. For this purpose we developed a study model represented by two proteins belonging to the CP family: CP, the founder protein produced by Ceratocystis platani, and the CP-orthologous cerato-populin (Pop1) produced by C. populicola. Both CP and Pop1 have been purified, cloned in P. pastoris, expressed, and characterized for their ability to aggregate. They are well-structured α/β proteins (the 3D-structure of CP has been recently determined), and have only the 70.1% of the amino acids identical or highly conserved. Moreover, they behave as PAMPs, since it stimulated plants to activate defense responses able to reduce consistently the fungal growth. Their capability to elicit differently defense events and their role in fungal physiology is under study.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
