Abstract

One of the major components of the staphylococcal biofilm is surface proteins that assemble as scaffold components of the biofilm matrix. Among the different surface proteins able to contribute to biofilm formation, this review is dedicated to the Biofilm Associated Protein (Bap). Bap is part of the accessory genome of Staphylococcus aureus but orthologs of Bap in other staphylococcal species belong to the core genome. When present, Bap promotes adhesion to abiotic surfaces and induces strong intercellular adhesion by self-assembling into amyloid like aggregates in response to the levels of calcium and the pH in the environment. During infection, Bap enhances the adhesion to epithelial cells where it binds directly to the host receptor Gp96 and inhibits the entry of the bacteria into the cells. To perform such diverse range of functions, Bap comprises several domains, and some of them include several motifs associated to distinct functions. Based on the knowledge accumulated with the Bap protein of S. aureus, this review aims to summarize the current knowledge of the structure and properties of each domain of Bap and their contribution to Bap functionality.

Highlights

  • Biofilm associated protein (Bap) was identified during the analysis of biofilm defective transposon insertion mutants in the bovine mastitis isolate, Staphylococcus aureus V329 (Cucarella et al, 2001)

  • Most of the available information has been obtained on the Biofilm Associated Protein (Bap) protein of S. aureus, but it is assumed that conclusions drawn from studies with this protein can most likely be applied to other Bap orthologs

  • An early study aiming to determine the role of calcium in Bap functionality revealed that concentrations equivalent to those present in the milk (~10 mM) inhibit Bap-mediated bacterial aggregation and biofilm formation (Arrizubieta et al, 2004)

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Summary

INTRODUCTION

Biofilm associated protein (Bap) was identified during the analysis of biofilm defective transposon insertion mutants in the bovine mastitis isolate, Staphylococcus aureus V329 (Cucarella et al, 2001). Sequencing of the bap gene surrounding region revealed that Bap was contained in a pathogenicity island (SaPIbov2; Ubeda et al, 2003). Structure and Function of Bap Domains the presence of Bap orthologs in many different bacterial species (Lasa and Penadés, 2006). The bap genes are carried in mobile genetic elements. There is no indication that the bap locus is carried on a mobile genetic element in some staphylococcal species such as Staphylococcus epidermidis, Staphylococcus simulans, Staphylococcus chromogenes, and Staphylococcus warneri. There is still very little knowledge about the function of a large part of Bap protein and how different domains of. Most of the available information has been obtained on the Bap protein of S. aureus, but it is assumed that conclusions drawn from studies with this protein can most likely be applied to other Bap orthologs

MULTIDOMAINS OF THE Bap PROTEIN
Number repeats
Structure and Function of Bap Domains B
ROLE OF Bap IN PATHOGENESIS
Findings
FINAL REMARKS

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