Mammalian cell entry gene family of Mycobacterium tuberculosis

Zhang, Xiancui; Xie, Jianping

doi:10.1007/s11010-011-0733-5

Cited by 73 publications

(94 citation statements)

References 47 publications

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“…Proteins-Mammalian cell entry (Mce) family proteins are crucial for the virulence of mycobacteria and represent components of transport systems that interact with host cells (68). Structural analysis has indicated that some Mce proteins are similar to colicins or ß-barrel porins, which form channels through lipid bilayers (69).…”

Section: Mammalian Cell Entry Familymentioning

confidence: 99%

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Analysis of the Secretome and Identification of Novel Constituents from Culture Filtrate of Bacillus Calmette-Guérin Using High-resolution Mass Spectrometry

Zheng

Ren

Wei

et al. 2013

Molecular & Cellular Proteomics

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Tuberculosis (TB) is an infectious bacterial disease that causes morbidity and mortality, especially in developing countries. Although its efficacy against TB has displayed a high degree of variability (0%-80%) in different trials, Mycobacterium bovis bacillus Calmette-Gué rin (BCG) has been recognized as an important weapon for preventing TB worldwide for over 80 years. Because secreted proteins often play vital roles in the interaction between bacteria and host cells, the secretome of mycobacteria is considered to be an attractive reservoir of potential candidate antigens for the development of novel vaccines and diagnostic reagents. In this study, we performed a proteomic analysis of BCG culture filtrate proteins using SDS-PAGE and high-resolution Fourier transform mass spectrometry. In total, 239 proteins (1555 unique peptides) were identified, including 185 secreted proteins or lipoproteins. Furthermore, 17 novel protein products not annotated in the BCG database were detected and validated by means of RT-PCR at the transcriptional level. Additionally, the translational start sites of 52 proteins were confirmed, and 22 proteins were validated through extension of the translational start sites based on N-terminus-derived peptides. There are 103 secreted proteins that have not been reported in previous studies on the mycobacterial secretome and are unique to our study. The physicochemical characteristics of the secreted proteins were determined. Major components from the culture superna-

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Section: Mammalian Cell Entry Familymentioning

confidence: 99%

“…Most interestingly, mce family genes are absent from the human genome. Therefore, Mce proteins might represent ideal candidate drug targets for better TB therapeutics (68).…”

Section: Mammalian Cell Entry Familymentioning

confidence: 99%

Analysis of the Secretome and Identification of Novel Constituents from Culture Filtrate of Bacillus Calmette-Guérin Using High-resolution Mass Spectrometry

Zheng

Ren

Wei

et al. 2013

Molecular & Cellular Proteomics

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“…MMP9 has enzymatic activity required for the development of the hallmark inflammatory granulomatous tissue reaction in the host (106). Next, intracellular invasion is mediated by phagocytosis or macropinocytosis in an Mce protein family-dependent manner, involving direct molecular interaction with the host, although the targeted host proteins are still unknown (107,108).…”

Section: Function and Interaction Of Individual Proteins And Complexesmentioning

confidence: 99%

Mycobacterium tuberculosisin the Proteomics Era

et al. 2014

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The emerging field of proteomics has contributed greatly to improving our understanding of the human pathogen Mycobacterium tuberculosis over the last two decades. In this chapter we provide a comprehensive overview of mycobacterial proteome research and highlight key findings. First, studies employing a combination of two-dimensional gel electrophoresis and mass spectrometry (MS) provided insights into the proteomic composition, initially of the whole bacillus and subsequently of subfractions, such as the cell wall, cytosol, and secreted proteins. Comparison of results obtained under various culture conditions, i.e., acidic pH, nutrient starvation, and low oxygen tension, aiming to mimic facets of the intracellular lifestyle of M. tuberculosis, provided initial clues to proteins relevant for intracellular survival and manipulation of the host cell. Further attempts were aimed at identifying the biological functions of the hypothetical M. tuberculosis proteins, which still make up a quarter of the gene products of M. tuberculosis, and at characterizing posttranslational modifications. Recent technological advances in MS have given rise to new methods such as selected reaction monitoring (SRM) and data-independent acquisition (DIA). These targeted, cutting-edge techniques combined with a public database of specific MS assays covering the entire proteome of M. tuberculosis allow the simple and reliable detection of any mycobacterial protein. Most recent studies attempt not only to identify but also to quantify absolute amounts of single proteins in the complex background of host cells without prior sample fractionation or enrichment. Finally, we will discuss the potential of proteomics to advance vaccinology, drug discovery, and biomarker identification to improve intervention and prevention measures for tuberculosis.

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“…Interestingly, unlike rapidly growing mycobacteria, our analysis of the M. phlei genome showed that this genome encodes a putative mammalian cell entry (MCE) operon, which was previously shown to be conserved only among slow-growing mycobacteria. This virulence factor operon in nonpathogenic Escherichia coli confers the ability to invade and survive inside host cells, such as macrophages and HeLa cells (3,13). Further genomic and functional analyses are needed to investigate this observation.…”

mentioning

confidence: 99%