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Review
. 2022 Dec 2;11(12):2397.
doi: 10.3390/antiox11122397.

Bacterial Protein Tyrosine Phosphatases as Possible Targets for Antimicrobial Therapies in Response to Antibiotic Resistance

Alicja Kuban-Jankowska  1 , Tomasz Kostrzewa  1 , Magdalena Gorska-Ponikowska  1   2   3
Affiliations
Review

Bacterial Protein Tyrosine Phosphatases as Possible Targets for Antimicrobial Therapies in Response to Antibiotic Resistance

Alicja Kuban-Jankowska et al. Antioxidants (Basel). .

Abstract

The review is focused on the bacterial protein tyrosine phosphatases (PTPs) utilized by bacteria as virulence factors necessary for pathogenicity. The inhibition of bacterial PTPs could contribute to the arrest of the bacterial infection process. This mechanism could be utilized in the design of antimicrobial therapy as adjuvants to antibiotics. The review summaries knowledge on pathogenic bacterial protein tyrosine phosphatases (PTPs) involved in infection process, such as: PTPA and PTPB from Staphylococcus aureus and Mycobacterium tuberculosis; SptP from Salmonella typhimurium; YopH from Yersinia sp. and TbpA from Pseudomonas aeruginosa. The review focuses also on the potential inhibitory compounds of bacterial virulence factors and inhibitory mechanisms such as the reversible oxidation of tyrosine phosphatases.

Keywords: antimicrobial therapy; bacterial phosphatase; protein tyrosine phosphatase; reversible oxidation; virulence factor.

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Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
Phosphatases as virulence factors of Yersinia spp.
Figure 2
Figure 2
Inactivation of tyrosine phosphatase by oxidation of the catalytic cysteine residue to sufenic, sulfinic or sulfonic acid.
See this image and copyright information in PMC

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