Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy

Bacterial adhesion is the first and a significant step in establishing infection. This adhesion normally occurs in presence of flow of fluids. Therefore, bacterial adhesins must be able to provide high strength interactions with their target surface in order to maintain the adhered bacteria under hy...

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Autores principales: Arnal, Laura, Longo, Gabriel Sebastián, Stupar, P., Castez, Marcos Federico, Cattelan, Natalia, Salvarezza, Roberto Carlos, Yantorno, Osvaldo Miguel, Kasas, S., Vela, María Elena
Formato: Articulo Preprint
Lenguaje:Inglés
Publicado: 2015
Materias:
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/120398
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id I19-R120-10915-120398
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Química
Bacteria
Biofilms
Force spectroscopy
Molecular recognition
Adhesins
spellingShingle Química
Bacteria
Biofilms
Force spectroscopy
Molecular recognition
Adhesins
Arnal, Laura
Longo, Gabriel Sebastián
Stupar, P.
Castez, Marcos Federico
Cattelan, Natalia
Salvarezza, Roberto Carlos
Yantorno, Osvaldo Miguel
Kasas, S.
Vela, María Elena
Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
topic_facet Química
Bacteria
Biofilms
Force spectroscopy
Molecular recognition
Adhesins
description Bacterial adhesion is the first and a significant step in establishing infection. This adhesion normally occurs in presence of flow of fluids. Therefore, bacterial adhesins must be able to provide high strength interactions with their target surface in order to maintain the adhered bacteria under hydromechanical stressing conditions. In the case of B. pertussis, a Gram-negative bacterium responsible of pertussis, a highly contagious human respiratory tract infection, an important protein participating in the adhesion process is a 220 KDa adhesin named Filamentous haemagglutinin (FHA), an outer membrane and also secreted protein that contains recognition domains to adhere to ciliated respiratory epithelial cells and macrophages. In this work, we obtained information of the cell-surface localization and distribution of the B. pertussis adhesin FHA using an antibody-functionalized AFM tip. Through the analysis of specific molecular recognition events we built a map of the spatial distribution of the adhesin which revealed a non-homogenous pattern. Moreover, our experiments showed a force induced reorganization of the adhesin in the surface of the cells, which could explain a reinforced adhesive response under external forces. This single-molecule information contributes to the understanding of basic molecular mechanisms used by bacterial pathogens to cause infectious disease and to gain insight into the structural features by which adhesins can act as force sensors under mechanical shear conditions.
format Articulo
Preprint
author Arnal, Laura
Longo, Gabriel Sebastián
Stupar, P.
Castez, Marcos Federico
Cattelan, Natalia
Salvarezza, Roberto Carlos
Yantorno, Osvaldo Miguel
Kasas, S.
Vela, María Elena
author_facet Arnal, Laura
Longo, Gabriel Sebastián
Stupar, P.
Castez, Marcos Federico
Cattelan, Natalia
Salvarezza, Roberto Carlos
Yantorno, Osvaldo Miguel
Kasas, S.
Vela, María Elena
author_sort Arnal, Laura
title Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
title_short Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
title_full Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
title_fullStr Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
title_full_unstemmed Localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
title_sort localization of adhesins on the surface of a pathogenic bacterial envelope through atomic force microscopy
publishDate 2015
url http://sedici.unlp.edu.ar/handle/10915/120398
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