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PMID: 9730978 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Localisation of Nramp1 in macrophages: modulation with activation and infection.

Journal of cell science ·Vol. 111 ( Pt 19) ·1998-10-00 ·Pages 2855-66

Searle S, Bright NA, Roach TI, Atkinson PG, Barton CH, Meloen RH, Blackwell JM

Abstract

The murine natural resistance-associated macrophage protein, Nramp1, has multiple pleiotropic effects on macrophage activation and regulates survival of intracellular pathogens including Leishmania, Salmonella and Mycobacterium species. Nramp1 acts as an iron transporter, but precisely how this relates to macrophage activation and/or pathogen survival remains unclear. To gain insight into function, anti-Nramp1 monoclonal and polyclonal antibodies are used here to localise Nramp1 following activation and infection. Confocal microscope analysis in uninfected macrophages demonstrates that both the mutant (infection-susceptible) and wild-type (infection-resistant) forms of the protein localise to the membranes of intracellular vesicular compartments. Gold labelling and electron microscopy defines these compartments more precisely as electron-lucent late endosomal and electron-dense lysosomal compartments, with Nramp1 colocalizing with Lamp1 and cathepsins D and L in both compartments, with macrosialin in late endosomes, and with BSA-5 nm gold in pre-loaded lysosomes. Nramp1 is upregulated with interferon-(gamma) and lipopolysaccaride treatment, coinciding with an increase in labelling in lysosomes relative to late endosomes and apparent dispersion of Nramp1-positive vesicles from a perinuclear location towards the periphery of the cytoplasm along the microtubular network. In both control and activated macrophages, expression of the protein is 3- to 4-fold higher in wild-type compared to mutant macrophages. In Leishmania major-infected macrophages, Nramp1 is observed in the membrane of the pathogen-containing phagosomes, which retain a perinuclear localization in resting macrophages. In Mycobacterium avium-infected resting and activated macrophages, Nramp1-positive vesicles migrated to converge, but not always fuse, with pathogen-containing phagosomes. The Nramp1 protein is thus located where it can have a direct influence on phagosome fusion and the microenvironment of the pathogen, as well as in the more general regulation of endosomal/lysosomal function in macrophages.

MeSH Terms
Amino Acid Sequence Animals Antibodies, Monoclonal Carrier Proteins/genetics,immunology,metabolism Cation Transport Proteins Cell Line Endosomes/metabolism Epitope Mapping Leishmania major/immunology,pathogenicity Lysosomes/metabolism Macrophage Activation Macrophages/immunology,metabolism,parasitology Membrane Proteins/genetics,immunology,metabolism Mice Microscopy, Confocal Microscopy, Immunoelectron Molecular Sequence Data Mutation Mycobacterium avium/immunology,pathogenicity
Chemicals
Antibodies, Monoclonal Carrier Proteins Cation Transport Proteins Membrane Proteins natural resistance-associated macrophage protein 1
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Searle S
Department of Medicine, University of Cambridge Clinical School, Level 5, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QQ, UK. [email protected].
Bright N A
Roach T I
Atkinson P G
Barton C H
Meloen R H
Blackwell J M
Article Info
Journal
Journal of cell science
Abbr.
J Cell Sci
ISSN
0021-9533
Published
1998-10-00
Pages
2855-66
Language
English
Region
England
NLM ID
0052457
Subset
IM
Grants
Wellcome Trust · United Kingdom
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