Lipoproteins of Mycobacterium tuberculosis : an abundant and functionally diverse class of cell envelope components

Sutcliffe, Iain and Harrington, Dean (2004) Lipoproteins of Mycobacterium tuberculosis : an abundant and functionally diverse class of cell envelope components. FEMS Microbiology Reviews, 28 (5). pp. 645-659. ISSN 0168-6445

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Official URL: http://dx.doi.org/10.1016/j.femsre.2004.06.002

Abstract

Mycobacterium tuberculosis remains the predominant bacterial scourge of mankind. Understanding of its biology and pathogenicity has been greatly advanced by the determination of whole genome sequences for this organism. Bacterial lipoproteins are a functionally diverse class of membrane-anchored proteins. The signal peptides of these proteins direct their export and post-translational lipid modification. These signal peptides are amenable to bioinformatic analysis, allowing the lipoproteins encoded in whole genomes to be catalogued. This review applies bioinformatic methods to the identification and functional characterisation of the lipoproteins encoded in the M. tuberculosis genomes. Ninety nine putative lipoproteins were identified and so this family of proteins represents ca. 2.5% of the M. tuberculosis predicted proteome. Thus, lipoproteins represent an important class of cell envelope proteins that may contribute to the virulence of this major pathogen.

Item Type: Article
Additional Information: Co-authored the paper and carried out the experimental work that makes a significant and original reanalysis of the Mycobacterium tuberculosis genome. Led to the definition of a family of proteins representing ca. 2.0% of the genome and which are likely to be of significance in understanding the pathogenesis of tuberculosis.
Uncontrolled Keywords: bioinformatics, genome, lipoprotein, periplasm, virulence factor
Subjects: F100 Chemistry
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: EPrint Services
Date Deposited: 07 Jan 2009 15:36
Last Modified: 17 Dec 2023 12:01
URI: https://nrl.northumbria.ac.uk/id/eprint/2638

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