Proteomic characterization of Mycobacterium tuberculosis reveals potential targets of bostrycin

Yuan, Peibo; He, Lei; Chen, Dongni; Sun, Yunhao; Ge, Zhenhuang; Dong, Shen; Lü, Yongjun

doi:10.1016/j.jprot.2019.103576

Cited by 11 publications

(4 citation statements)

References 54 publications

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“…For LC-MS/MS proteomics analysis, prior studies utilized combinations of lysis buffers, beads, and a sonication step to break open mycobacterial cells and extract proteins. However, these studies mostly focused on the protein profiling and identification without further accounting for the biosafety properties of the approach ( 28 , 29 ). In the current study, we showed that heat inactivation treatment produced satisfactory protein preservation for downstream proteomics assays.…”

Section: Discussionmentioning

confidence: 99%

Biosafety and Proteome Profiles of Different Heat Inactivation Methods for Mycobacterium tuberculosis

et al. 2021

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Inactivation of Mycobacterium tuberculosis is an important step to guarantee biosafety for subsequent M. tuberculosis identification and related research, notably in areas of endemicity with minimal resources. However, certain biomolecules might be denatured or hydrolyzed because of the harsh inactivation process, and a standardized protocol is yet to be determined.

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Section: Discussionmentioning

confidence: 99%

Biosafety and Proteome Profiles of Different Heat Inactivation Methods for Mycobacterium tuberculosis

et al. 2021

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“…Bostrycin was also able to inhibit the growth of Mycobacterium tuberculosis in vitro and inhibit the activity of effector protein tyrosine phosphatase (MptpB) secreted by Mtb. In addition, bostrycin also acted as an antitumor agent against various cancer cell lines [206][207][208][209]. Both toxins showed a phytotoxic effect on water hyacinth at a concentration of 7 and 30 µg•mL −1 , respectively [128].…”

Section: Anthraquinone Derivativesmentioning

confidence: 99%

Recent Advances in Alternaria Phytotoxins: A Review of Their Occurrence, Structure, Bioactivity, and Biosynthesis

Wang

Guo

Luo

et al. 2022

JoF

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Alternaria is a ubiquitous fungal genus in many ecosystems, consisting of species and strains that can be saprophytic, endophytic, or pathogenic to plants or animals, including humans. Alternaria species can produce a variety of secondary metabolites (SMs), especially low molecular weight toxins. Based on the characteristics of host plant susceptibility or resistance to the toxin, Alternaria phytotoxins are classified into host-selective toxins (HSTs) and non-host-selective toxins (NHSTs). These Alternaria toxins exhibit a variety of biological activities such as phytotoxic, cytotoxic, and antimicrobial properties. Generally, HSTs are toxic to host plants and can cause severe economic losses. Some NHSTs such as alternariol, altenariol methyl-ether, and altertoxins also show high cytotoxic and mutagenic activities in the exposed human or other vertebrate species. Thus, Alternaria toxins are meaningful for drug and pesticide development. For example, AAL-toxin, maculosin, tentoxin, and tenuazonic acid have potential to be developed as bioherbicides due to their excellent herbicidal activity. Like altersolanol A, bostrycin, and brefeldin A, they exhibit anticancer activity, and ATX V shows high activity to inhibit the HIV-1 virus. This review focuses on the classification, chemical structure, occurrence, bioactivity, and biosynthesis of the major Alternaria phytotoxins, including 30 HSTs and 50 NHSTs discovered to date.

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“…Proteomic analysis was performed as we previously described (61,65). In brief, for each sample, 100 μg of protein was reduced with 10 mM DTT at 37 • C for 45 min, and iodoacetamide was then added to a final concentration of 15 mM, with incubation at room temperature for 1 h in the dark.…”

Section: Proteomic Analysis (Lc-ms)mentioning

confidence: 99%

New Global Insights on the Regulation of the Biphasic Life Cycle and Virulence Via ClpP-Dependent Proteolysis in Legionella pneumophila

Yuan

Chen

et al. 2022

Molecular & Cellular Proteomics

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Proteomic characterization of Mycobacterium tuberculosis reveals potential targets of bostrycin

Cited by 11 publications

References 54 publications

Biosafety and Proteome Profiles of Different Heat Inactivation Methods for Mycobacterium tuberculosis

Biosafety and Proteome Profiles of Different Heat Inactivation Methods for Mycobacterium tuberculosis

Recent Advances in Alternaria Phytotoxins: A Review of Their Occurrence, Structure, Bioactivity, and Biosynthesis

New Global Insights on the Regulation of the Biphasic Life Cycle and Virulence Via ClpP-Dependent Proteolysis in Legionella pneumophila

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