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The polymer and materials science of the bacterial fimbriae Caf1

Lookup NU author(s): Dr David Fulton, Dr Gema Dura, Dr Daniel PetersORCiD

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

© 2023 The Royal Society of Chemistry. Fimbriae are long filamentous polymeric protein structures located upon the surface of bacteria. Often implicated in pathogenicity, the biosynthesis and function of fimbriae has been a productive topic of study for many decades. Evolutionary pressures have ensured that fimbriae possess unique structural and mechanical properties which are advantageous to bacteria. These properties are also difficult to engineer with well-known synthetic and natural fibres, and this has raised an intriguing question: can we exploit the unique properties of bacterial fimbriae in useful ways? Initial work has set out to explore this question by using Capsular antigen fragment 1 (Caf1), a fimbriae expressed naturally by Yersina pestis. These fibres have evolved to ‘shield’ the bacterium from the immune system of an infected host, and thus are rather bioinert in nature. Caf1 is, however, very amenable to structural mutagenesis which allows the incorporation of useful bioactive functions and the modulation of the fibre's mechanical properties. Its high-yielding recombinant synthesis also ensures plentiful quantities of polymer are available to drive development. These advantageous features make Caf1 an archetype for the development of new polymers and materials based upon bacterial fimbriae. Here, we cover recent advances in this new field, and look to future possibilities of this promising biopolymer.


Publication metadata

Author(s): Fulton DA, Dura G, Peters DT

Publication type: Review

Publication status: Published

Journal: Biomaterials Science

Year: 2023

Volume: 22

Issue: 11

Pages: 7229-7246

Online publication date: 26/09/2023

Acceptance date: 22/09/2023

ISSN (print): 2047-4830

ISSN (electronic): 2047-4849

Publisher: Royal Society of Chemistry

URL: https://doi.org/10.1039/d3bm01075a

DOI: 10.1039/d3bm01075a

PubMed id: 37791425


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