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Structure. 2016 Oct 4;24(10):1788-1794. doi: 10.1016/j.str.2016.07.009. Epub 2016 Aug 25.

Mycobacterium tuberculosis LppM Displays an Original Structure and Domain Composition Linked to a Dual Localization.

Author information

1
Centre de Biochimie Structurale, CNRS UMR 5048, Inserm U1054, Université de Montpellier, 29 rue de Navacelles, 34090 Montpellier, France.
2
University of Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 8204 - CIIL - Center for Infection and Immunity of Lille, 59000 Lille, France.
3
Institut de Pharmacologie et de Biologie Structurale, Université de Toulouse, CNRS, UPS, 31400 Toulouse, France.
4
Centre de Biochimie Structurale, CNRS UMR 5048, Inserm U1054, Université de Montpellier, 29 rue de Navacelles, 34090 Montpellier, France. Electronic address: martin@cbs.cnrs.fr.

Abstract

Mycobacterium tuberculosis (Mtb) encodes several bacterial effectors impacting the colonization of phagocytes. LppM (Rv2171) is both implicated in phagocytosis and able to efficiently block phagosomal acidification in the macrophage, two key processes contributing to Mtb persistence. We show that LppM is anchored to the mycobacterial cell wall by a C-terminal membrane domain. However, the protein also exists as a truncated protein secreted into the culture medium. The LppM solution structure we solve here displays no similarity with other Mtb lipoproteins also involved in phagosomal maturation (i.e., LprG). In addition, we demonstrate that the protein may be able to bind rare molecular species of phosphatidylinositol mannosides, bacterial compounds known to affect the host immune response. Thus, our data demonstrate a dual localization of LppM and provide a unique perspective on the regulation of protein secretion and localization in Mtb.

PMID:
27568926
DOI:
10.1016/j.str.2016.07.009
[Indexed for MEDLINE]
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