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Significance One major defense mechanism of mycobacteria relies mainly on the synthesis and transport of specialized lipids, processes that reside in the cell wall. Among the transporters, Mycobacterial membrane protein Large (MmpL) plays an essential role. We describe the role of MmpL8 (MmpL8MAB ) in the survival ofMycobacterium abscessus within eukaryotic hosts. We show that its absence slows the contact betweenM. abscessus and the host cell cytosol, an essential element in its resistance to the cell bactericidal mechanisms. The absence of MmpL8MAB leads to reduced production of a previously unknown glycolipid: a glycosyl diacylated nonadecyl diol (GDND). The glycolipid seems unique to theMycobacterium chelonae complex, supporting the view that GDND might represent a typical signature ofM. abscessus infection.

MmpL8 MAB controls Mycobacterium abscessus virulence and production of a previously unknown glycolipid family

MmpL8 _MAB controls Mycobacterium abscessus virulence and production of a previously unknown glycolipid family