BACKGROUND: The "cerato-platanin family" consists of fungal-secreted proteins that are involved in various stages of the host-fungus interaction and act as phytotoxins, elicitors of defense responses and allergens. Cerato-platanin (CP) is a moderately hydrophobic protein secreted and localized in the cell wall of Ceratocystis platani, the causal agent of a severe disease of Platanus. These properties make CP like the hydrophobins: these are self-assembling proteins that form a surface coating which is involved in the formation of aerial hyphae and in adherence to surfaces. METHODS: CP aggregation was monitored by ThT, circular dichroism, and AFM. The eliciting activity of CP aggregates was assayed on leaves and cells. RESULTS: The CP self-assembles forming amyloid-like aggregates via a nucleated growth mechanism which is joined up with a cleavage of the N-terminus. The ovoidal shape and the lack of a clear transition toward an all-beta structure distinguish these aggregates from typical amyloid fibrils. Moreover, CP aggregates interact with hydrophobic surfaces and enhance the hypersensitive response of Platanus. CONCLUSION AND GENERAL SIGNIFICANCE: CP forms "ordered aggregates" for which the soluble prefibrillar structures are the end point of the aggregation process, and do not evolve to insoluble fibrils. An involvement in host-microbe interaction is also suggested.
BACKGROUND: The "cerato-platanin family" consists of fungal-secreted proteins that are involved in various stages of the host-fungus interaction and act as phytotoxins, elicitors of defense responses and allergens. Cerato-platanin (CP) is a moderately hydrophobic protein secreted and localized in the cell wall of Ceratocystis platani, the causal agent of a severe disease of Platanus. These properties make CP like the hydrophobins: these are self-assembling proteins that form a surface coating which is involved in the formation of aerial hyphae and in adherence to surfaces. METHODS: CP aggregation was monitored by ThT, circular dichroism, and AFM. The eliciting activity of CP aggregates was assayed on leaves and cells. RESULTS: The CP self-assembles forming amyloid-like aggregates via a nucleated growth mechanism which is joined up with a cleavage of the N-terminus. The ovoidal shape and the lack of a clear transition toward an all-beta structure distinguish these aggregates from typical amyloid fibrils. Moreover, CP aggregates interact with hydrophobic surfaces and enhance the hypersensitive response of Platanus. CONCLUSION AND GENERAL SIGNIFICANCE: CP forms "ordered aggregates" for which the soluble prefibrillar structures are the end point of the aggregation process, and do not evolve to insoluble fibrils. An involvement in host-microbe interaction is also suggested.
Authors: Aline L de Oliveira; Mariana Gallo; Luigia Pazzagli; Celso E Benedetti; Gianni Cappugi; Aniello Scala; Barbara Pantera; Alberto Spisni; Thelma A Pertinhez; Daniel O Cicero Journal: J Biol Chem Date: 2011-03-30 Impact factor: 5.157
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Authors: Eddy Patricia Lopez Molano; Odalys García Cabrera; Juliana Jose; Leandro Costa do Nascimento; Marcelo Falsarella Carazzolle; Paulo José Pereira Lima Teixeira; Javier Correa Alvarez; Ricardo Augusto Tiburcio; Paulo Massanari Tokimatu Filho; Gustavo Machado Alvares de Lima; Rafael Victório Carvalho Guido; Thamy Lívia Ribeiro Corrêa; Adriana Franco Paes Leme; Piotr Mieczkowski; Gonçalo Amarante Guimarães Pereira Journal: BMC Genomics Date: 2018-01-17 Impact factor: 3.969