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. 2017 Oct 24;8:1368. doi: 10.3389/fimmu.2017.01368

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Copyright © 2017 Uribe-Querol and Rosales.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Inhibition of phagosome maturation. (a) Several pathogens, such as Mycobacterium tuberculosis (161), Histoplasma capsulatum (182), and Rhodococcus equi (183) inhibit acidification by preventing the accumulation of V-ATPase on the phagosome membrane. M. tuberculosis also blocks early endosome antigen 1 (EEA1) on the membrane (165), while Neisseria gonorrhoeae express a porin that induces large amounts of Rab5 (186) and also proteases that digest lysosomal-associated membrane proteins (LAMPs) (187). Another bacteria, Streptococcus pyogenes, express the virulence factor M1, which regulates vesicle trafficking (188). Each of these actions effectively will block lysosome fusion to the phagosome. (b) Other pathogens, such as Legionella pneumophila (189, 190) and Brucella melitensis (191), induce the rapid association of the phagosome with the endoplasmic reticulum (ER). (c) The bacteria Coxiella burnetti (192, 193), and the parasite Leishmania reside inside a phagolysosome-like vesicle known as parasitophorous vacuole (PV) that concentrates Rab5 on the membrane. Leishmania promastigotes also insert lipophosphoglycan (LPG) into the phagosome membrane (194). These actions, in consequence, prevent lysosome fusion (195).