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PMID: 11207624 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Evidence that Dot-dependent and -independent factors isolate the Legionella pneumophila phagosome from the endocytic network in mouse macrophages.

Cellular microbiology ·Vol. 3 ·No. 2 ·2001-02-00 ·Pages 99-114

Joshi AD, Sturgill-Koszycki S, Swanson MS

Abstract

Legionella pneumophila survives within macrophages by evading phagosome-lysosome fusion. To determine whether L. pneumophila resides in an intermediate endosomal compartment or is isolated from the endosomal pathway and to investigate what bacterial factors contribute to establishment of its vacuole, we applied a series of fluorescence microscopy assays. The majority of vacuoles, aged 2.5 min to 4 h containing post-exponential phase (PE) L. pneumophila, appeared to be separate from the endosomal pathway, as judged by the absence of transferrin receptor, LAMP-1, cathepsin D and each of four fluorescent probes used to label the endocytic pathway either before or after infection. In contrast, more than 70% of phagosomes that contained Escherichia coli, polystyrene beads, or exponential phase (E) L. pneumophila matured to phagolysosomes, as judged by co-localization with LAMP-1, cathepsin D and fluorescent endosomal probes. Surprisingly, neither bacterial viability nor the putative Dot/Icm transport complex was absolutely required for vacuole isolation; although phagosomes containing either formalin-killed PE wild-type or live PE dotA or dotB mutant L. pneumophila rapidly accumulated LAMP-1, less than 20% acquired lysosomal cathepsin D or fluorescent endosomal probes. Therefore, a Dot-dependent factor(s) isolates the L. pneumophila phagosome from a LAMP-1-containing compartment, and a formalin-resistant Dot-independent activity inhibits vacuolar accumulation of endocytosed material and delivery to the degradative lysosomes.

MeSH Terms
Animals Antigens, CD/metabolism Biomarkers Cathepsin D/metabolism Endoscopes Female Legionella pneumophila/pathogenicity Lysosome-Associated Membrane Glycoproteins Lysosomes Macrophages/microbiology Membrane Glycoproteins/metabolism Mice Models, Biological Molecular Probes Phagosomes/microbiology Receptors, Transferrin/metabolism Transport Vesicles/microbiology
Chemicals
Antigens, CD Biomarkers Lysosome-Associated Membrane Glycoproteins Membrane Glycoproteins Molecular Probes Receptors, Transferrin Cathepsin D
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Joshi A D
Department of Microbiology and Immunology, The University of Michigan Medical School, Ann Arbor 48109, USA.
Sturgill-Koszycki S
Swanson M S
Article Info
Journal
Cellular microbiology
Abbr.
Cell Microbiol
ISSN
1462-5814
Published
2001-02-00
Pages
99-114
Language
English
Region
England
NLM ID
100883691
Subset
IM
Grants
NIAID NIH HHS · R29AI40694-01BM · United States
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