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

Authors
  • De Maio, Flavio1, 2
  • Berisio, Rita3
  • Manganelli, Riccardo4
  • Delogu, Giovanni2, 5
  • 1 Dipartimento di Scienze di Laboratorio e Infettivologiche, Fondazione Policlinico Universitario "A. Gemelli" , Rome, Italy. , (Italy)
  • 2 Dipartimento di Scienze Biotecnologiche di Base, Cliniche Intensivologiche e Perioperatorie - Sezione di Microbiologia, Università Cattolica del Sacro Cuore , Rome, Italy. , (Italy)
  • 3 Institute of Bio-Structures and Bio-Imaging - CNR-IBB , Naples, Italy. , (Italy)
  • 4 Department of Molecular Medicine, University of Padova , Padua, Italy. , (Italy)
  • 5 Mater Olbia Hospital , Olbia, Italy. , (Italy)
Type
Published Article
Journal
Virulence
Publisher
Landes Bioscience
Publication Date
Dec 01, 2020
Volume
11
Issue
1
Pages
898–915
Identifiers
DOI: 10.1080/21505594.2020.1785815
PMID: 32713249
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

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.

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