Exploring coaggregation mechanisms involved in biofilm formation in drinking water through a proteomic-based approach

Author:

Afonso Ana C1234,Simões Manuel12ORCID,Saavedra Maria José3,Simões Lúcia4,Lema Juan M5,Trueba-Santiso Alba5ORCID

Affiliation:

1. LEPABE—Laboratory for Process Engineering, Environment, Biotechnology and Energy, Faculty of Engineering, University of Porto , Rua Dr Roberto Frias, 4200-465 Porto , Portugal

2. ALiCE—Associate Laboratory in Chemical Engineering, Faculty of Engineering, University of Porto , Rua Dr Roberto Frias, 4200-465 Porto , Portugal

3. CITAB, Department of Veterinary Sciences, University of Trás-os-Montes e Alto Douro , 5000-801 Vila Real , Portugal

4. CEB-LABBELS, University of Minho, Campus de Gualtar , 4710-057 Braga , Portugal

5. CRETUS, Department of Chemical Engineering, University of Santiago de Compostela, Campus Vida , 15782 Santiago de Compostela, Galicia , Spain

Abstract

Abstract Aim Coaggregation, a highly specific cell–cell interaction mechanism, plays a pivotal role in multispecies biofilm formation. While it has been mostly studied in oral environments, its occurrence in aquatic systems is also acknowledged. Considering biofilm formation’s economic and health-related implications in engineered water systems, it is crucial to understand its mechanisms. Here, we hypothesized that traceable differences at the proteome level might determine coaggregation ability. Methods and Results Two strains of Delftia acidovorans, isolated from drinking water were studied. First, in vitro motility assays indicated more swarming and twitching motility for the coaggregating strain (C+) than non-coaggregating strain (C−). By transmission electronic microscopy, we confirmed the presence of flagella for both strains. By proteomics, we detected a significantly higher expression of type IV pilus twitching motility proteins in C+, in line with the motility assays. Moreover, flagellum ring proteins were more abundant in C+, while those involved in the formation of the flagellar hook (FlE and FilG) were only detected in C−. All the results combined suggested structural and conformational differences between stains in their cell appendages. Conclusion This study presents an alternative approach for identifying protein biomarkers to detect coaggregation abilities in uncharacterized strains.

Funder

Galician Competitive Research Group

Juan de la Cierva-Formación

Histology and Electron Microscopy

FCT

MCTES

Publisher

Oxford University Press (OUP)

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