Uncovering new signaling proteins and potential drug targets through the interactome analysis of Mycobacterium tuberculosis

Cui, Tao; Zhang, Lei; Wang, Xizhou; He, Zheng‐Guo

doi:10.1186/1471-2164-10-118

Cited by 87 publications

(84 citation statements)

References 47 publications

(51 reference statements)

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“…However, due to the overexpression of DcpA, some amounts of protein were also detected in the other fraction. Considering the reports of Mawuenyega et al (2005) and Cui et al (2009), the presence of the protein in the other cellular fraction (cytosol) can be detected when the membrane sites are saturated. Also, it is known that a protein can be detected in the membrane fraction after differential centrifugation only if it is associated with it (Delogu et al, 2004;Gibbons et al, 2007;Rezwan et al, 2007).…”

Section: Dual-active Dcpa and C-di-gmp Turnovermentioning

confidence: 99%

“…Using membrane proteome analysis, Mawuenyega et al (2005) reported that Rv1354c (an orthologue of DcpA in M. tuberculosis) is present in the membrane fraction. Subsequently, Cui et al (2009) showed that Rv1354c interacts with the ATP-binding cassette (ABC) transporter in the membrane. To examine the cellular distribution of DcpA, the protein sequence was first analysed using the TMHMM tool and then the PSORTb tool.…”

Section: Dual-active Dcpa and C-di-gmp Turnovermentioning

confidence: 99%

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Characterization of a dual-active enzyme, DcpA, involved in cyclic diguanosine monophosphate turnover in Mycobacterium smegmatis

et al. 2014

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We have reported previously that the long-term survival of Mycobacterium smegmatis is facilitated by a dual-active enzyme MSDGC-1 (renamed DcpA), which controls the cellular turnover of cyclic diguanosine monophosphate (c-di-GMP). Most mycobacterial species possess at least a single copy of a DcpA orthologue that is highly conserved in terms of sequence similarity and domain architecture. Here, we show that DcpA exists in monomeric and dimeric forms. The dimerization of DcpA is due to non-covalent interactions between two protomers that are arranged in a parallel orientation. The dimer shows both synthesis and hydrolysis activities, whereas the monomer shows only hydrolysis activity. In addition, we have shown that DcpA is associated with the cytoplasmic membrane and exhibits heterogeneous cellular localization with a predominance at the cell poles. Finally, we have also shown that DcpA is involved in the change in cell length and colony morphology of M. smegmatis. Taken together, our study provides additional evidence about the role of the bifunctional protein involved in c-di-GMP signalling in M. smegmatis.

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Section: Dual-active Dcpa and C-di-gmp Turnovermentioning

confidence: 99%

Section: Dual-active Dcpa and C-di-gmp Turnovermentioning

confidence: 99%

Characterization of a dual-active enzyme, DcpA, involved in cyclic diguanosine monophosphate turnover in Mycobacterium smegmatis

et al. 2014

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“…PPIs forms the basis of cellular events such as signaling, regulation, and other processes [3,26], therefore the most highly connected proteins are usually the most important and are considered to participate extensively in cellular processes [27] these comprises networks that can be predicted computationally that leverage the large amount of sequences data generated recently [26]. It would be expected that the highly connected proteins are chaperones, especially in MTB facing hostile environmental factors [3].…”

Section: Interactions and Lcrmentioning

confidence: 99%

“…Having high guanine + cytosine content that reflected in biased amino acids in the proteins [2]. It expressed unique mechanisms to stand different stresses [3], through the proteins which are the main catalysts, structural components and signaling messengers, they are the machines of a biological system [4].…”

Section: Introductionmentioning

confidence: 99%

Exploitation of Hub Proteins as Drug Targets for Mycobacterium Tuberculosis H37rv

Jalil

2017

Asian J Pharm Clin Res

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Objective: Mycobacterium tuberculosis (TB), a causative agent of TB, increased the resistance to most drugs in use and coinfection with HIV. It needs the new drug(s), the latter should be special candidate targets.Methods: Hub proteins were studied (Rv2198c, Rv2507, and Rv3763) which had very high connected partners. These were modeled to be used for screening chemical databases. Results:The proteins were found to be with increased low-complexity regions especially at the amino ends, they exhibited primary level (layers) of interactions and involved in secondary and more levels of interactions. Conclusions:The proteins with high interacting partners would be good targets as their disruption will disturb the cellular functions. The chosen targets (Rv2198c, Rv2507, and Rv3763) have very high interactions at a different level (layers), they were modeled to be used in survey of chemical databases.

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“…Based on the variation in the critical network parameter values the potentiality of the targets was determined. Target protein interacting with more proteins is considered as metabolically important active protein, which can act as an appropriate drug target [30][31].…”

Section: Fig 1 Percentage Distribution Of Sub-cellular Locations In mentioning

confidence: 99%

In Silico Identification and Characterization of Potent Drug Targets in Fungal Pathogen causing Keratitis

Rashmi¹

2018

IJRASET

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Availability of genome sequences of pathogens has provided a tremendous amount of information that can be useful in drug target identification. Subtractive proteomics approach is being used to mine the list of proteins present in different Aspergillus species which are non-homologous to human and essential for the survival of the pathogen. Current study is based on complete proteome information of Aspergillus terreus strain NIH 2624available in biological databases to identify putative protein targets. Subjecting the total set of pathogen non homologous proteins (10402) against the Database of Essential Genes 2030 proteins were screened out as essential proteins of the Aspergillus terreus,out of which 136 are found to be essential in the pathogen with no human homolog. Among 136 proteins; around 88 proteins were found to be putative uncharacterized using CELLO. The hypothetical essential proteins were functionally annotated through SVMProt server. Druggability of each of the identified drug targets was also evaluated by the Drug Bank database.

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Uncovering new signaling proteins and potential drug targets through the interactome analysis of Mycobacterium tuberculosis

Abstract: Background: Analysis of the pathogen interactome is a powerful approach for dissecting potential signal transduction and virulence pathways. It also offers opportunities for exploring new drug targets.

Cited by 87 publications

References 47 publications

Characterization of a dual-active enzyme, DcpA, involved in cyclic diguanosine monophosphate turnover in Mycobacterium smegmatis

Characterization of a dual-active enzyme, DcpA, involved in cyclic diguanosine monophosphate turnover in Mycobacterium smegmatis

Exploitation of Hub Proteins as Drug Targets for Mycobacterium Tuberculosis H37rv

In Silico Identification and Characterization of Potent Drug Targets in Fungal Pathogen causing Keratitis

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