NDLI: Atomic force microscopy images suggest aggregation mechanism in cerato-platanin

Content Provider	Springer Nature Link
Author	Sbrana, F. Bongini, L. Cappugi, G. Fanelli, D. Guari, A. Pazzagli, L. Scala, A. Vassalli, M. Zoppi, C. Tiribilli, B.
Copyright Year	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.
Starting Page	727
Ending Page	732
Page Count	6
File Format	PDF
ISSN	01757571
Journal	European Biophysics Journal
Volume Number	36
Issue Number	7
e-ISSN	14321017
Language	English
Publisher	Springer-Verlag
Publisher Date	2007-04-12
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Protein aggregation Cerato-platanin AFM Neurobiology Animal Physiology Plant Physiology Biochemistry Cell Biology Biophysics/Biomedical Physics
Content Type	Text
Resource Type	Article
Subject	Medicine Biophysics

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