A communal bacterial adhesin anchors biofilm and bystander cells to surfaces

Autor: Katrina L. Van Dellen, Paula I. Watnick, Cedric Absalon
Jazyk: angličtina
Rok vydání: 2011
Předmět:
Zdroj: PLoS Pathogens, Vol 7, Iss 8, p e1002210 (2011)
PLoS Pathogens
ISSN: 1553-7374
1553-7366
Popis: While the exopolysaccharide component of the biofilm matrix has been intensively studied, much less is known about matrix-associated proteins. To better understand the role of these proteins, we undertook a proteomic analysis of the V. cholerae biofilm matrix. Here we show that the two matrix-associated proteins, Bap1 and RbmA, perform distinct roles in the biofilm matrix. RbmA strengthens intercellular attachments. In contrast, Bap1 is concentrated on surfaces where it serves to anchor the biofilm and recruit cells not yet committed to the sessile lifestyle. This is the first example of a biofilm-derived, communally synthesized conditioning film that stabilizes the association of multilayer biofilms with a surface and facilitates recruitment of planktonic bystanders to the substratum. These studies define a novel paradigm for spatial and functional differentiation of proteins in the biofilm matrix and provide evidence for bacterial cooperation in maintenance and expansion of the multilayer biofilm.
Author Summary The bacterial multilayer biofilm consists of matrix-enclosed cells attached to each other to form large aggregates. The base of these aggregates may be attached to a living or non-living surface. The biofilm matrix most often contains at least one exopolysaccharide component and may also contain protein and DNA. While much is known about the exopolysaccharide component of the Gram-negative biofilm matrix, little is known about the function of biofilm matrix proteins. We hypothesized that the biofilm matrix might harbor proteins with diverse functions. Therefore, we undertook the first proteomic analysis of the biofilm matrix of a Gram-negative bacterium, V. cholerae. We subsequently focused on Bap1 and RbmA, two proteins that are abundant in the biofilm matrix. RbmA, which strengthens intercellular interactions, was found to be evenly distributed in the biofilm. In contrast, communally synthesized Bap1 was concentrated at the biofilm-surface interface and stabilized the association of the multilayer biofilm with the surface. Furthermore, the addition of purified Bap1 increased attachment of free-swimming cells to a surface. These studies provide evidence for spatial and functional differentiation of proteins in the biofilm matrix and suggest bacterial cooperation in stabilization of multilayer biofilm surface association and recruitment of new members.
Databáze: OpenAIRE