Literature DB >> 22459131

Chaperone-dependent mechanisms for acid resistance in enteric bacteria.

Weizhe Hong1, Ye E Wu, Xinmiao Fu, Zengyi Chang.   

Abstract

The extremely acidic environment of the mammalian stomach not only serves to facilitate food digestion but also acts as a natural barrier against infections of food-borne pathogens. Many pathogenic bacteria, such as enterohemorrhagic Escherichia coli, can breach this host defense and cause severe diseases. These pathogens have evolved multiple intricate strategies to overcome the bactericidal activity of acids. In particular, recent studies have uncovered the central roles of two periplasmic chaperones, HdeA and HdeB, in protecting enteric bacteria from extremely acidic conditions. Here, we review recent advances in the understanding of the acid resistance mechanisms of Gram-negative bacteria and focus on the mechanisms of HdeA and HdeB in preventing acid-induced protein aggregation and facilitating protein refolding following pH neutralization.
Copyright © 2012 Elsevier Ltd. All rights reserved.

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Year:  2012        PMID: 22459131     DOI: 10.1016/j.tim.2012.03.001

Source DB:  PubMed          Journal:  Trends Microbiol        ISSN: 0966-842X            Impact factor:   17.079


  43 in total

1.  The complex role of the N-terminus and acidic residues of HdeA as pH-dependent switches in its chaperone function.

Authors:  Sayuri Pacheco; Marlyn A Widjaja; Jafaeth S Gomez; Karin A Crowhurst; Ravinder Abrol
Journal:  Biophys Chem       Date:  2020-05-19       Impact factor: 2.352

2.  Identification of putative substrates for the periplasmic chaperone YfgM in Escherichia coli using quantitative proteomics.

Authors:  Hansjörg Götzke; Claudio Muheim; A F Maarten Altelaar; Albert J R Heck; Gianluca Maddalo; Daniel O Daley
Journal:  Mol Cell Proteomics       Date:  2014-11-17       Impact factor: 5.911

3.  HdeB functions as an acid-protective chaperone in bacteria.

Authors:  Jan-Ulrik Dahl; Philipp Koldewey; Loïc Salmon; Scott Horowitz; James C A Bardwell; Ursula Jakob
Journal:  J Biol Chem       Date:  2014-11-12       Impact factor: 5.157

Review 4.  Biogenesis, quality control, and structural dynamics of proteins as explored in living cells via site-directed photocrosslinking.

Authors:  Xinmiao Fu; Zengyi Chang
Journal:  Protein Sci       Date:  2019-05-10       Impact factor: 6.725

5.  Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone.

Authors:  Xing-Chi Yu; Yunfei Hu; Jienv Ding; Hongwei Li; Changwen Jin
Journal:  J Biol Chem       Date:  2018-12-20       Impact factor: 5.157

6.  How bacteria survive an acid trip.

Authors:  Karan S Hingorani; Lila M Gierasch
Journal:  Proc Natl Acad Sci U S A       Date:  2013-03-25       Impact factor: 11.205

7.  Chaperone activation by unfolding.

Authors:  Linda Foit; Jenny S George; Bin W Zhang; Charles L Brooks; James C A Bardwell
Journal:  Proc Natl Acad Sci U S A       Date:  2013-03-04       Impact factor: 11.205

Review 8.  Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge.

Authors:  Karan S Hingorani; Lila M Gierasch
Journal:  Curr Opin Struct Biol       Date:  2014-01-14       Impact factor: 6.809

Review 9.  Recent advances in understanding enteric pathogenic Escherichia coli.

Authors:  Matthew A Croxen; Robyn J Law; Roland Scholz; Kristie M Keeney; Marta Wlodarska; B Brett Finlay
Journal:  Clin Microbiol Rev       Date:  2013-10       Impact factor: 26.132

Review 10.  Survival of the Fittest: How Bacterial Pathogens Utilize Bile To Enhance Infection.

Authors:  Jeticia R Sistrunk; Kourtney P Nickerson; Rachael B Chanin; David A Rasko; Christina S Faherty
Journal:  Clin Microbiol Rev       Date:  2016-10       Impact factor: 26.132

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