Next Article in Journal
Bacillus subtilis DSM 32315 Supplementation Attenuates the Effects of Clostridium perfringens Challenge on the Growth Performance and Intestinal Microbiota of Broiler Chickens
Next Article in Special Issue
Mycobacterium abscessus: Environmental Bacterium Turned Clinical Nightmare
Previous Article in Journal
Defining Kinetic Properties of HIV-Specific CD8+ T-Cell Responses in Acute Infection
Previous Article in Special Issue
Mycobacterium smegmatis But Not Mycobacterium avium subsp. hominissuis Causes Increased Expression of the Long Non-Coding RNA MEG3 in THP-1-Derived Human Macrophages and Associated Decrease of TGF-β
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessReview

MmpL Proteins in Physiology and Pathogenesis of M. tuberculosis

Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR 97239, USA
Author to whom correspondence should be addressed.
Microorganisms 2019, 7(3), 70;
Received: 15 January 2019 / Revised: 14 February 2019 / Accepted: 3 March 2019 / Published: 5 March 2019
(This article belongs to the Special Issue Virulence Studies of Pathogenic Mycobacteria of Humans and Animal)
PDF [1282 KB, uploaded 5 March 2019]


Mycobacterium tuberculosis (Mtb) remains an important human pathogen. The Mtb cell envelope is a critical bacterial structure that contributes to virulence and pathogenicity. Mycobacterial membrane protein large (MmpL) proteins export bulky, hydrophobic substrates that are essential for the unique structure of the cell envelope and directly support the ability of Mtb to infect and persist in the host. This review summarizes recent investigations that have enabled insight into the molecular mechanisms underlying MmpL substrate export and the role that these substrates play during Mtb infection. View Full-Text
Keywords: Mycobacterium tuberculosis; lipids; MmpL; lipid transport; cell envelope Mycobacterium tuberculosis; lipids; MmpL; lipid transport; cell envelope

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

Share & Cite This Article

MDPI and ACS Style

Melly, G.; Purdy, G.E. MmpL Proteins in Physiology and Pathogenesis of M. tuberculosis. Microorganisms 2019, 7, 70.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Microorganisms EISSN 2076-2607 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top