Abstract
Universal stress proteins are ubiquitously expressed in bacteria, archaea and plants and other eukaryotes. A general property of USPs is their role in adaptation of bacteria to oxidative stress, high temperature, low pH and/or hypoxia. There is increasing evidence that these proteins facilitate the adaption of bacterial pathogens to the human host environment, thereby facilitating colonisation and pathogenicity. USPs in Mycobacterium tuberculosis are well studied and may play a role in latency of tuberculosis. USP expressed by Acinetobacter baumannii, Listeria monocytogenes and Salmonella enterica serovar Typhimurium are involved in survival in vivo, while USPs expressed in Pseudomonas aeruginosa and Porphyromonas gingivalis are involved in biofilm formation. Burkholderia cepacia complex and Staphylococcus aureus express USPs that play roles in host cell or host protein adhesion. There is also increasing evidence that USPs also bind to antimicrobial agents and may be ideal candidates to target in the future design of new anti-virulence strategies.
Keywords: Universal stress proteins, UspA, latency, hypoxia, oxidative stress, bacterial infection.
Current Medicinal Chemistry
Title:The Role of Universal Stress Proteins in Bacterial Infections
Volume: 24 Issue: 36
Author(s): Andrew O’Connor and Siobhán McClean*
Affiliation:
- School of Biomolecular and Biomedical Science, University College Dublin, Dublin,Ireland
Keywords: Universal stress proteins, UspA, latency, hypoxia, oxidative stress, bacterial infection.
Abstract: Universal stress proteins are ubiquitously expressed in bacteria, archaea and plants and other eukaryotes. A general property of USPs is their role in adaptation of bacteria to oxidative stress, high temperature, low pH and/or hypoxia. There is increasing evidence that these proteins facilitate the adaption of bacterial pathogens to the human host environment, thereby facilitating colonisation and pathogenicity. USPs in Mycobacterium tuberculosis are well studied and may play a role in latency of tuberculosis. USP expressed by Acinetobacter baumannii, Listeria monocytogenes and Salmonella enterica serovar Typhimurium are involved in survival in vivo, while USPs expressed in Pseudomonas aeruginosa and Porphyromonas gingivalis are involved in biofilm formation. Burkholderia cepacia complex and Staphylococcus aureus express USPs that play roles in host cell or host protein adhesion. There is also increasing evidence that USPs also bind to antimicrobial agents and may be ideal candidates to target in the future design of new anti-virulence strategies.
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Cite this article as:
O’Connor Andrew and McClean Siobhán *, The Role of Universal Stress Proteins in Bacterial Infections, Current Medicinal Chemistry 2017; 24 (36) . https://dx.doi.org/10.2174/0929867324666170124145543
DOI https://dx.doi.org/10.2174/0929867324666170124145543 |
Print ISSN 0929-8673 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-533X |
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