Abstract
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-β 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.
| Original language | English |
|---|---|
| Pages (from-to) | 1334-1344 |
| Number of pages | 11 |
| Journal | BBA - General Subjects |
| Volume | 1790 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - Oct 2009 |
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Keywords
- Amyloid-like assemblage
- Cerato-platanin family
- Fungal protein
- Host-microbe interaction
- Hydrophobin
- Protein aggregation
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Characterization of ordered aggregates of cerato-platanin and their involvement in fungus-host interactions. / Pazzagli, Luigia; Zoppi, Camilla; Carresi, Lara; Tiribilli, Bruno; Sbrana, Francesca; Schiff, Silvia; Pertinhez, Thelma A.; Scala, Aniello; Cappugi, Gianni.
In: BBA - General Subjects, Vol. 1790, No. 10, 10.2009, p. 1334-1344.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterization of ordered aggregates of cerato-platanin and their involvement in fungus-host interactions
AU - Pazzagli, Luigia
AU - Zoppi, Camilla
AU - Carresi, Lara
AU - Tiribilli, Bruno
AU - Sbrana, Francesca
AU - Schiff, Silvia
AU - Pertinhez, Thelma A.
AU - Scala, Aniello
AU - Cappugi, Gianni
PY - 2009/10
Y1 - 2009/10
N2 - 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-β 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.
AB - 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-β 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.
KW - Amyloid-like assemblage
KW - Cerato-platanin family
KW - Fungal protein
KW - Host-microbe interaction
KW - Hydrophobin
KW - Protein aggregation
UR - http://www.scopus.com/inward/record.url?scp=70049101499&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=70049101499&partnerID=8YFLogxK
U2 - 10.1016/j.bbagen.2009.07.014
DO - 10.1016/j.bbagen.2009.07.014
M3 - Article
C2 - 19631724
AN - SCOPUS:70049101499
VL - 1790
SP - 1334
EP - 1344
JO - Biochimica et Biophysica Acta - General Subjects
JF - Biochimica et Biophysica Acta - General Subjects
SN - 0304-4165
IS - 10
ER -