PE is a functional domain responsible for protein translocation and localization on mycobacterial cell wall

Alessandro Cascioferro, Giovanni Delogu, Marisa Colone, Michela Sali, Annarita Stringaro, Giuseppe Arancia, Giovanni Fadda, Giorgio Palù, Riccardo Manganelli

Research output: Contribution to journalArticlepeer-review

Abstract

The PE family of Mycobacterium tuberculosis includes 98 proteins which share a highly homologous N-terminus sequence of about 110 amino acids (PE domain). Depending on the C-terminal domain, the PE family can be divided in three subfamilies, the largest of which is the PE_PGRS with 61 members. In this study, we determined the cellular localization of three PE proteins by cell fractionation and immunoelectron microscopy by expressing chimeric epitope-tagged recombinant proteins in Mycobacterium smegmatis. We demonstrate that the PE domain of PE_PGRS33 and PE11 (a protein constituted by the only PE domain) contains the information necessary for cell wall localization, and that they can be used as N-terminal fusion partners to deliver a sufficiently long C-terminus-linked protein domain on the mycobacterial cell surface. Indeed, we demonstrate that PE_PGRS33 and Rv3097c (a lipase belonging to the PE family) are surface exposed and localize in the mycobacterial cell wall. Moreover, we found that PE_PGRS33 is easily extractable by detergents suggesting its localization in the mycobacterial outer membrane. Beyond defining the cellular localization of these proteins, and a function for their PE domains, these data open the interesting possibility to construct recombinant mycobacteria expressing heterologous antigens on their surface for vaccine purposes.

Original languageEnglish
Pages (from-to)1536-1547
Number of pages12
JournalMolecular Microbiology
Volume66
Issue number6
DOIs
Publication statusPublished - Dec 2007

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

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