Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro

Hingley‐Wilson, Suzie; Lougheed, Kathryn; Ferguson, K.; Leiva, Sergio; Williams, Huw D.

doi:10.1016/j.tube.2010.03.013

Cited by 65 publications

(62 citation statements)

References 73 publications

(81 reference statements)

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“…All other USPs have either two tandem USP domains or are associated with other domains of unknown function. The single USP present in Mycobacterium leprae, ML1390, is the ortholog of Rv1636 sharing 89% identity (55). Shown in Fig.…”

Section: Discussionmentioning

confidence: 99%

A Universal Stress Protein (USP) in Mycobacteria Binds cAMP

Banerjee

Adolph

Gopalakrishnapai

et al. 2015

Journal of Biological Chemistry

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Background: Mycobacteria utilize cAMP for regulating transcription and protein acetylation. Results: We identify and structurally characterize a universal stress protein as an abundant and specific cAMP-binding protein. Conclusion:The USP domain is a novel cAMP-binding module. Significance: Certain members of the universal stress protein family serve to sequester cAMP, acting as sinks to regulate the availability of cAMP for downstream effectors.

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Section: Discussionmentioning

confidence: 99%

A Universal Stress Protein (USP) in Mycobacteria Binds cAMP

Banerjee

Adolph

Gopalakrishnapai

et al. 2015

Journal of Biological Chemistry

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“…The role of USPs in response to several stress conditions was better elucidated in other bacteria, including Escherichia coli (Gustavsson et al, 2002; Nachin et al, 2005) and Salmonella typhimurium (Liu et al, 2007; Bangera et al, 2015), Haemophilus influenzae (Fleischmann et al, 1995; Sousa and McKay, 2001), Mycobacterium tuberculosis (O'Toole and Williams, 2003; Drumm et al, 2009), Pseudomonas aeruginosa (Boes et al, 2008), and Lactobacillus plantarum (Licandro-Seraut et al, 2008; Gury et al, 2009). In all cases, the expression of USP has been associated to the arrest of cellular growth in response to prolonged stress (Hingley-Wilson et al, 2010). Nyström and Neidhardt (1992, 1994) showed that the survival of E. coli was reduced in the uspA -mutated strains.…”

Section: Discussionmentioning

confidence: 99%

Homology-Based Modeling of Universal Stress Protein from Listeria innocua Up-Regulated under Acid Stress Conditions

et al. 2016

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An Universal Stress Protein (USP) expressed under acid stress condition by Listeria innocua ATCC 33090 was investigated. The USP was up-regulated not only in the stationary phase but also during the exponential growth phase. The three dimensional (3D) structure of USP was predicted using a combined proteomic and bioinformatics approach. Phylogenetic analysis showed that the USP from Listeria detected in our study was distant from the USPs of other bacteria (such as Pseudomonas spp., Escherichia coli, Salmonella spp.) and clustered in a separate and heterogeneous class including several USPs from Listeria spp. and Lactobacillus spp. An important information on the studied USP was obtained from the 3D-structure established through the homology modeling procedure. In detail, the Model_USP-691 suggested that the investigated USP had a homo-tetrameric quaternary structure. Each monomer presented an architecture analogous to the Rossmann-like α/β-fold with five parallel β-strands, and four α-helices. The analysis of monomer-monomer interfaces and quality of the structure alignments confirmed the model reliability. In fact, the structurally and sequentially conserved hydrophobic residues of the β-strand 5 (in particular the residues V146 and V148) were involved in the inter-chains contact. Moreover, the highly conserved residues I139 and H141 in the region α4 were involved in the dimer association and functioned as hot spots into monomer–monomer interface assembly. The hypothetical assembly of dimers was also supported by the large interface area and by the negative value of solvation free energy gain upon interface interaction. Finally, the structurally conserved ATP-binding motif G-2X-G-9X-G(S/T-N) suggested for a putative role of ATP in stabilizing the tetrameric assembly of the USP. Therefore, the results obtained from a multiple approach, consisting in the application of kinetic, proteomic, phylogenetic and modeling analyses, suggest that Listeria USP could be considered a new type of ATP-binding USP involved in the response to acid stress condition during the exponential growth phase.

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“…These reports provide further evidence that UspA may be an important component of and even mechanistically linked to many different stress responses. The tuberculosis genome contains 10 different Usp-type proteins with apparent functional redundancy, but data suggest that there may be incomplete redundancy of particular Usp proteins for different stresses (65,66). The data linking Rv2623 to chronic infection indicate this protein may have a specific importance in the infection process that cannot be replicated by other Usp proteins.…”

Section: Resultsmentioning

confidence: 99%

A Proteomic Signature of Dormancy in the Actinobacterium Micrococcus luteus

et al. 2017

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Dormancy is a protective state in which diverse bacteria, including Mycobacterium tuberculosis, Staphylococcus aureus, Treponema pallidum (syphilis), and Borrelia burgdorferi (Lyme disease), curtail metabolic activity to survive external stresses, including antibiotics. Evidence suggests dormancy consists of a continuum of interrelated states, including viable but nonculturable (VBNC) and persistence states. VBNC and persistence contribute to antibiotic tolerance, reemergence from latent infections, and even quorum sensing and biofilm formation. Previous studies indicate that the protein mechanisms regulating persistence and VBNC states are not well understood. We have queried the VBNC state of Micrococcus luteus NCTC 2665 (MI-2665) by quantitative proteomics combining gel electrophoresis, high-performance liquid chromatography, and tandem mass spectrometry to elucidate some of these mechanisms. MI-2665 is a nonpathogenic actinobacterium containing a small (2.5-Mb), high-GC-content genome which exhibits a well-defined VBNC state induced by nutrient deprivation. The MI-2665 VBNC state demonstrated a loss of protein diversity accompanied by increased levels of 18 proteins that are conserved across actinobacteria, 14 of which have not been previously identified in VNBC. These proteins implicate an anaplerotic strategy in the transition to VBNC, including changes in the glyoxylate shunt, redox and amino acid metabolism, and ribosomal regulatory processes. Our data suggest that MI-2665 is a viable model for dissecting the protein mechanisms underlying the VBNC stress response and provide the first protein-level signature of this state. We expect that this protein signature will enable future studies deciphering the protein mechanisms of dormancy and identify novel therapeutic strategies effective against antibiotictolerant bacterial infections.IMPORTANCE Dormancy is a protective state enabling bacteria to survive antibiotics, starvation, and the immune system. Dormancy is comprised of different states, including persistent and viable but nonculturable (VBNC) states that contribute to the spread of bacterial infections. Therefore, it is imperative to identify how bacteria utilize these different dormancy states to survive antibiotic treatment. The objective of our research is to eliminate dormancy as a route to antibiotic tolerance by understanding the proteins that control dormancy in Micrococcus luteus NCTC 2665. This bacterium has unique advantages for studying dormancy, including a small genome and a well-defined and reproducible VBNC state. Our experiments implicate four previously identified and 14 novel proteins upregulated in VBNC that may regulate this critical survival mechanism.KEYWORDS antibiotic tolerance, proteomics, stress response, systems biology D ormancy is a remarkable stress response in which bacteria curtail metabolic activity to survive potentially fatal external stresses. Dormancy has broad implications for many pathogenic bacteria, including Mycobacterium tuberculosis, Staphylococcus ...

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Individual Mycobacterium tuberculosis universal stress protein homologues are dispensable in vitro

Cited by 65 publications

References 73 publications

A Universal Stress Protein (USP) in Mycobacteria Binds cAMP

A Universal Stress Protein (USP) in Mycobacteria Binds cAMP

Homology-Based Modeling of Universal Stress Protein from Listeria innocua Up-Regulated under Acid Stress Conditions

A Proteomic Signature of Dormancy in the Actinobacterium Micrococcus luteus

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