Literature DB >> 22817724

Exploiting amyloid: how and why bacteria use cross-β fibrils.

Elizabeth B Sawyer1, Dennis Claessen, Sally L Gras, Sarah Perrett.   

Abstract

Many bacteria produce protein fibrils that are structurally analogous to those associated with protein misfolding diseases such as Alzheimer's disease. However, unlike fibrils associated with disease, bacterial amyloids have beneficial functions including conferring stability to biofilms, regulating development or imparting virulence. In the present review, we consider what makes amyloid fibrils so suitable for these roles and discuss recent developments in the study of bacterial amyloids, in particular the chaplins from Streptomyces coelicolor. We also consider the broader impact of the study of bacterial amyloids on our understanding of infection and disease and on developments in nanotechnology.

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Year:  2012        PMID: 22817724     DOI: 10.1042/BST20120013

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  10 in total

Review 1.  Amyloid Structures as Biofilm Matrix Scaffolds.

Authors:  Agustina Taglialegna; Iñigo Lasa; Jaione Valle
Journal:  J Bacteriol       Date:  2016-09-09       Impact factor: 3.490

2.  On the evolutionary trajectories of signal-transducing amyloids in fungi and beyond.

Authors:  Asen Daskalov
Journal:  Prion       Date:  2016-09-02       Impact factor: 3.931

3.  Pre-amyloid oligomers of the proteotoxic RepA-WH1 prionoid assemble at the bacterial nucleoid.

Authors:  María Moreno-Del Álamo; Susana Moreno-Díaz de la Espina; M Elena Fernández-Tresguerres; Rafael Giraldo
Journal:  Sci Rep       Date:  2015-10-01       Impact factor: 4.379

4.  Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry.

Authors:  Xiao-Ming Zhou; Ulyana Shimanovich; Therese W Herling; Si Wu; Christopher M Dobson; Tuomas P J Knowles; Sarah Perrett
Journal:  ACS Nano       Date:  2015-06-08       Impact factor: 15.881

Review 5.  Interaction of the Human Contact System with Pathogens-An Update.

Authors:  Sonja Oehmcke-Hecht; Juliane Köhler
Journal:  Front Immunol       Date:  2018-02-26       Impact factor: 7.561

6.  Direct Observation of Oligomerization by Single Molecule Fluorescence Reveals a Multistep Aggregation Mechanism for the Yeast Prion Protein Ure2.

Authors:  Jie Yang; Alexander J Dear; Thomas C T Michaels; Christopher M Dobson; Tuomas P J Knowles; Si Wu; Sarah Perrett
Journal:  J Am Chem Soc       Date:  2018-02-07       Impact factor: 15.419

7.  Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.

Authors:  Elena Yarmola; Ivan P Ishkov; Nicholas M di Cologna; Megan Menashe; Robert L Whitener; Joanna R Long; Jacqueline Abranches; Stephen J Hagen; L Jeannine Brady
Journal:  Microbiol Spectr       Date:  2022-08-11

8.  Microanatomy at cellular resolution and spatial order of physiological differentiation in a bacterial biofilm.

Authors:  Diego O Serra; Anja M Richter; Gisela Klauck; Franziska Mika; Regine Hengge
Journal:  MBio       Date:  2013-03-19       Impact factor: 7.867

9.  Between Amyloids and Aggregation Lies a Connection with Strength and Adhesion.

Authors:  Peter N Lipke; Caleen Ramsook; Melissa C Garcia-Sherman; Desmond N Jackson; Cho X J Chan; Michael Bois; Stephen A Klotz
Journal:  New J Sci       Date:  2014

10.  Enhanced purification coupled with biophysical analyses shows cross-β structure as a core building block for Streptococcus mutans functional amyloids.

Authors:  Ana L Barran-Berdon; Sebastian Ocampo; Momin Haider; Joyce Morales-Aparicio; Gregory Ottenberg; Amy Kendall; Elena Yarmola; Surabhi Mishra; Joanna R Long; Stephen J Hagen; Gerald Stubbs; L Jeannine Brady
Journal:  Sci Rep       Date:  2020-03-20       Impact factor: 4.379

  10 in total

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