PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction

To the PE_PGRS protein subfamily belongs a group of surface-exposed mycobacterial antigens that in Mycobacterium tuberculosis (Mtb) H37Rv accounts to more than 65 genes, 51 of which are thought to express a functional protein. PE_PGRS proteins share a conserved structural architecture with three mai...

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Autores principales:	Flavio De Maio, Rita Berisio, Riccardo Manganelli, Giovanni Delogu
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2020
Materias:	pe/ppe proteins pe_pgrss mycobacterium tuberculosis mycobacterial envelope bacterial pathogenesis Infectious and parasitic diseases RC109-216
Acceso en línea:	https://doaj.org/article/09b5b7b629af4d77841a367e684d524f
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spelling	oai:doaj.org-article:09b5b7b629af4d77841a367e684d524f2021-11-17T14:21:58ZPE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction2150-55942150-560810.1080/21505594.2020.1785815https://doaj.org/article/09b5b7b629af4d77841a367e684d524f2020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1785815https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608To the PE_PGRS protein subfamily belongs a group of surface-exposed mycobacterial antigens that in Mycobacterium tuberculosis (Mtb) H37Rv accounts to more than 65 genes, 51 of which are thought to express a functional protein. PE_PGRS proteins share a conserved structural architecture with three main domains: the N-terminal PE domain; the PGRS domain, that can vary in sequence and size and is characterized by the presence of multiple GGA-GGX amino acid repeats; the highly conserved sequence containing the GRPLI motif that links the PE and PGRS domains; the unique C-terminus end that can vary in size from few to up to ≈ 300 amino acids. pe_pgrs genes emerged in slow-growing mycobacteria and expanded and diversified in MTBC and few other pathogenic mycobacteria. Interestingly, despite sequence homology and apparent redundancy, PE_PGRS proteins seem to have evolved a peculiar function. In this review, we summarize the actual knowledge on this elusive protein family in terms of evolution, structure, and function, focusing on the role of PE_PGRS in TB pathogenesis. We provide an original hypothesis on the role of the PE domain and propose a structural model for the polymorphic PGRS domain that might explain how so similar proteins can have different physiological functions.Flavio De MaioRita BerisioRiccardo ManganelliGiovanni DeloguTaylor & Francis Grouparticlepe/ppe proteinspe_pgrssmycobacterium tuberculosismycobacterial envelopebacterial pathogenesisInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 898-915 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	pe/ppe proteins pe_pgrss mycobacterium tuberculosis mycobacterial envelope bacterial pathogenesis Infectious and parasitic diseases RC109-216
spellingShingle	pe/ppe proteins pe_pgrss mycobacterium tuberculosis mycobacterial envelope bacterial pathogenesis Infectious and parasitic diseases RC109-216 Flavio De Maio Rita Berisio Riccardo Manganelli Giovanni Delogu PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
description	To the PE_PGRS protein subfamily belongs a group of surface-exposed mycobacterial antigens that in Mycobacterium tuberculosis (Mtb) H37Rv accounts to more than 65 genes, 51 of which are thought to express a functional protein. PE_PGRS proteins share a conserved structural architecture with three main domains: the N-terminal PE domain; the PGRS domain, that can vary in sequence and size and is characterized by the presence of multiple GGA-GGX amino acid repeats; the highly conserved sequence containing the GRPLI motif that links the PE and PGRS domains; the unique C-terminus end that can vary in size from few to up to ≈ 300 amino acids. pe_pgrs genes emerged in slow-growing mycobacteria and expanded and diversified in MTBC and few other pathogenic mycobacteria. Interestingly, despite sequence homology and apparent redundancy, PE_PGRS proteins seem to have evolved a peculiar function. In this review, we summarize the actual knowledge on this elusive protein family in terms of evolution, structure, and function, focusing on the role of PE_PGRS in TB pathogenesis. We provide an original hypothesis on the role of the PE domain and propose a structural model for the polymorphic PGRS domain that might explain how so similar proteins can have different physiological functions.
format	article
author	Flavio De Maio Rita Berisio Riccardo Manganelli Giovanni Delogu
author_facet	Flavio De Maio Rita Berisio Riccardo Manganelli Giovanni Delogu
author_sort	Flavio De Maio
title	PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
title_short	PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
title_full	PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
title_fullStr	PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
title_full_unstemmed	PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction
title_sort	pe_pgrs proteins of mycobacterium tuberculosis: a specialized molecular task force at the forefront of host–pathogen interaction
publisher	Taylor & Francis Group
publishDate	2020
url	https://doaj.org/article/09b5b7b629af4d77841a367e684d524f
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PE_PGRS proteins of Mycobacterium tuberculosis: A specialized molecular task force at the forefront of host–pathogen interaction

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