Cerato-platanin (CP), the first member of the ‘‘cerato-platanin family’’, is a moderately hydrophobic protein produced by Ceratocystis fimbriata, the causal agent of a severe plant disease called ‘‘canker stain’’. The protein is localized in the cell wall of the fungus and it seems to be involved in the host-plane interaction and induces both cell necrosis and phytoalexin synthesis (one of the first plant defence-related events). Recently, it has been determined that CP, like other fungal surface protein, is able to self assemble in vitro. In this paper we characterize the aggregates of CP by Atomic Force Microscopy (AFM) images. We observe that CP tends to form early annular-shaped oligomers that seem to constitute the fundamental bricks of a hierarchical aggregation process, eventually resulting in large macrofibrillar assemblies. A simple model, based on the hypothesis that the aggregation is energetically favourable when the exposed surface is reduced, is compatible with the measured aggregates’ shape and size. The proposed model can help to understand the mechanism by which CP and many other fungal surface proteins exert their effects.

Atomic force microscopy images suggest aggregation mechanism in cerato-platanin / F. SBRANA; L. BONGINI; G. CAPPUGI; D. FANELLI; A. GUARINO; L. PAZZAGLI; A. SCALA; M. VASSALLI; C. ZOPPI; B. TIRIBILLI. - In: EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS. - ISSN 0175-7571. - STAMPA. - 36(2007), pp. 727-732.

Atomic force microscopy images suggest aggregation mechanism in cerato-platanin.

CAPPUGI, GIANNI;FANELLI, DUCCIO;PAZZAGLI, LUIGIA;SCALA, ANIELLO;
2007

Abstract

Cerato-platanin (CP), the first member of the ‘‘cerato-platanin family’’, is a moderately hydrophobic protein produced by Ceratocystis fimbriata, the causal agent of a severe plant disease called ‘‘canker stain’’. The protein is localized in the cell wall of the fungus and it seems to be involved in the host-plane interaction and induces both cell necrosis and phytoalexin synthesis (one of the first plant defence-related events). Recently, it has been determined that CP, like other fungal surface protein, is able to self assemble in vitro. In this paper we characterize the aggregates of CP by Atomic Force Microscopy (AFM) images. We observe that CP tends to form early annular-shaped oligomers that seem to constitute the fundamental bricks of a hierarchical aggregation process, eventually resulting in large macrofibrillar assemblies. A simple model, based on the hypothesis that the aggregation is energetically favourable when the exposed surface is reduced, is compatible with the measured aggregates’ shape and size. The proposed model can help to understand the mechanism by which CP and many other fungal surface proteins exert their effects.
36
727
732
F. SBRANA; L. BONGINI; G. CAPPUGI; D. FANELLI; A. GUARINO; L. PAZZAGLI; A. SCALA; M. VASSALLI; C. ZOPPI; B. TIRIBILLI
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/256037
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