000133482 001__ 133482
000133482 005__ 20181203021432.0
000133482 037__ $$aARTICLE
000133482 245__ $$aBrucella abortus transits through the autophagic pathway and replicates in the endoplasmic reticulum of nonprofessional phagocytes
000133482 269__ $$a1998
000133482 260__ $$c1998
000133482 336__ $$aJournal Articles
000133482 500__ $$aCentre d'Immunologie INSERM-CNRS de Marseille-Luminy, Marseille, France.
000133482 520__ $$aBrucella abortus is an intracellular pathogen that replicates within a membrane-bounded compartment. In this study, we have examined the intracellular pathway of the virulent B. abortus strain 2308 (S2308) and the attenuated strain 19 (S19) in HeLa cells. At 10 min after inoculation, both bacterial strains are transiently detected in phagosomes characterized by the presence of early endosomal markers such as the early endosomal antigen 1. At approximately 1 h postinoculation, bacteria are located within a compartment positive for the lysosome-associated membrane proteins (LAMPs) and the endoplasmic reticulum (ER) marker sec61beta but negative for the mannose 6-phosphate receptors and cathepsin D. Interestingly, this compartment is also positive for the autophagosomal marker monodansylcadaverin, suggesting that S2308 and S19 are located in autophagic vacuoles. At 24 h after inoculation, attenuated S19 is degraded in lysosomes, while virulent S2308 multiplies within a LAMP- and cathepsin D-negative but sec61beta- and protein disulfide isomerase-positive compartment. Furthermore, treatment of infected cells with the pore-forming toxin aerolysin from Aeromonas hydrophila causes vacuolation of the bacterial replication compartment. These results are compatible with the hypothesis that pathogenic B. abortus exploits the autophagic machinery of HeLa cells to establish an intracellular niche favorable for its replication within the ER.
000133482 6531_ $$aAntigens
000133482 6531_ $$aCD/isolation & purification
000133482 6531_ $$aBrucella abortus/*growth & development/pathogenicity
000133482 6531_ $$aCathepsin D/isolation & purification
000133482 6531_ $$aCell Compartmentation
000133482 6531_ $$aEndoplasmic Reticulum/*microbiology
000133482 6531_ $$aHela Cells
000133482 6531_ $$aHuman
000133482 6531_ $$aMembrane Glycoproteins/isolation & purification
000133482 6531_ $$aModels
000133482 6531_ $$aBiological
000133482 6531_ $$aPhagocytes/*microbiology
000133482 6531_ $$aPhagosomes/*microbiology
000133482 6531_ $$aSupport
000133482 6531_ $$aNon-U.S. Gov't
000133482 6531_ $$aVacuoles
000133482 700__ $$aPizarro-Cerda, J.
000133482 700__ $$aMeresse, S.
000133482 700__ $$aParton, R. G.
000133482 700__ $$0240085$$g171549$$avan der Goot, G.
000133482 700__ $$aSola-Landa, A.
000133482 700__ $$aLopez-Goni, I.
000133482 700__ $$aMoreno, E.
000133482 700__ $$aGorvel, J. P.
000133482 773__ $$j66$$tInfect Immun$$k12$$q5711-24
000133482 909C0 $$xU11271$$0252037$$pVDG
000133482 909CO $$pSV$$particle$$ooai:infoscience.tind.io:133482
000133482 937__ $$aVDG-ARTICLE-1998-002
000133482 973__ $$rREVIEWED$$sPUBLISHED$$aOTHER
000133482 980__ $$aARTICLE