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.
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