Publication:
Staphylococcal Bap proteins build amyloid scaffold biofilm matrices in response to environmental signals

Consultable a partir de

Date

2016

Authors

Navarro, Susanna
Ventura, Salvador
Garnett, James A.
Matthews, Steve
Penadés, José R.

Director

Publisher

Public Library of Science
Acceso abierto / Sarbide irekia
Artículo / Artikulua
Versión publicada / Argitaratu den bertsioa

Project identifier

ES/6PN/AGL2011-23954
MINECO//BIO2014-53530-R/ES/
MINECO//BFU2013-44763-P/ES/

Abstract

Major components of the biofilm matrix scaffold are proteins that assemble to create a unified structure that maintain bacteria attached to each other and to surfaces. We provide evidence that a surface protein present in several staphylococcal species forms functional amyloid aggregates to build the biofilm matrix in response to specific environmental conditions. Under low Ca2+ concentrations and acidic pH, Bap is processed and forms insoluble aggregates with amyloidogenic properties. When the Ca2+ concentration increases, metal-coordinated Bap adopts a structurally more stable conformation and as a consequence, the N-terminal region is unable to assemble into amyloid aggregates. The control of Bap cleavage and assembly helps to regulate biofilm matrix development as a function of environmental changes.

Keywords

Staphylococcus aureus, Bacterial biofilms, Amyloid proteins, Extracellular matrix

Department

IdAB. Instituto de Agrobiotecnología / Agrobioteknologiako Institutua

Faculty/School

Degree

Doctorate program

Editor version

Funding entities

This research was supported by the Spanish Ministry of Economy and Competitiveness grants AGL2011-23954, BIO2014-53530-R and BFU2013-44763-P. JV was supported by Ramon y Cajal (RYC-2009-03948) contract from the Spanish Ministry of Economy and Competitiveness.

© 2016 Taglialegna et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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