Literature DB >> 16629660

Self-compartmentalized bacterial proteases and pathogenesis.

Susan M Butler1, Richard A Festa, Michael J Pearce, K Heran Darwin.   

Abstract

Protein degradation is required for homeostasis of all living organisms. Self-compartmentalized ATP-dependent proteases are required for virulence of several pathogenic bacteria. Among the proteases implicated are ClpP and Lon, as well as the more recently identified bacterial proteasome. It is generally assumed that when a pathogen invades a host, microbial proteins become irreversibly damaged and need to be degraded. However, recent data suggest that proteolysis is also essential for virulence gene regulation. In this review, we will discuss what is known about the relationship between ATP-dependent proteolysis and pathogenesis. In addition, we will propose other potential roles these chambered proteases may have in bacterial virulence. Importantly, these proteases show promise as targets for antimicrobial therapy.

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Year:  2006        PMID: 16629660     DOI: 10.1111/j.1365-2958.2006.05128.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  56 in total

1.  Mycobacterium tuberculosis serine protease Rv3668c can manipulate the host-pathogen interaction via Erk-NF-κB axis-mediated cytokine differential expression.

Authors:  Quanju Zhao; Wu Li; Tian Chen; Ying He; Wanyan Deng; Hongping Luo; Jianping Xie
Journal:  J Interferon Cytokine Res       Date:  2014-03-31       Impact factor: 2.607

2.  Regulation of host hemoglobin binding by the Staphylococcus aureus Clp proteolytic system.

Authors:  Allison J Farrand; Michelle L Reniere; Hanne Ingmer; Dorte Frees; Eric P Skaar
Journal:  J Bacteriol       Date:  2013-08-30       Impact factor: 3.490

3.  Specific protease activity indicates the degree of Pseudomonas aeruginosa infection in chronic infected wounds.

Authors:  D Wildeboer; K E Hill; F Jeganathan; D W Williams; A D Riddell; P E Price; D W Thomas; P Stephens; R A Abuknesha; R G Price
Journal:  Eur J Clin Microbiol Infect Dis       Date:  2012-01-26       Impact factor: 3.267

4.  The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring.

Authors:  Tatos Akopian; Olga Kandror; Ravikiran M Raju; Meera Unnikrishnan; Eric J Rubin; Alfred L Goldberg
Journal:  EMBO J       Date:  2012-01-27       Impact factor: 11.598

Review 5.  A camel passes through the eye of a needle: protein unfolding activity of Clp ATPases.

Authors:  Michal Zolkiewski
Journal:  Mol Microbiol       Date:  2006-09       Impact factor: 3.501

6.  Transcriptome analysis reveals that ClpXP proteolysis controls key virulence properties of Streptococcus mutans.

Authors:  Jessica K Kajfasz; Jacqueline Abranches; José A Lemos
Journal:  Microbiology (Reading)       Date:  2011-08-04       Impact factor: 2.777

7.  Examination of the nucleotide-linked assembly mechanism of E. coli ClpA.

Authors:  Elizabeth C Duran; Aaron L Lucius
Journal:  Protein Sci       Date:  2019-06-03       Impact factor: 6.725

8.  Identification of Burkholderia cenocepacia strain H111 virulence factors using nonmammalian infection hosts.

Authors:  Stephan Schwager; Kirsty Agnoli; Manuela Köthe; Friederike Feldmann; Michael Givskov; Aurelien Carlier; Leo Eberl
Journal:  Infect Immun       Date:  2012-10-22       Impact factor: 3.441

Review 9.  Using small molecules to dissect mechanisms of microbial pathogenesis.

Authors:  Aaron W Puri; Matthew Bogyo
Journal:  ACS Chem Biol       Date:  2009-08-21       Impact factor: 5.100

10.  Structural insights on the Mycobacterium tuberculosis proteasomal ATPase Mpa.

Authors:  Tao Wang; Hua Li; Gang Lin; Chunyan Tang; Dongyang Li; Carl Nathan; K Heran Darwin; Huilin Li
Journal:  Structure       Date:  2009-10-14       Impact factor: 5.006

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