ArticleInfection and immunity2006
Role of phagosomes and major histocompatibility complex class II (MHC-II) compartment in MHC-II antigen processing of Mycobacterium tuberculosis in human macrophages.
Article in Infection and immunity, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 48 citations in OpenAlex.
- Multiple genetic loci influence vaccine-induced protection against Mycobacterium tuberculosis in genetically diverse mice.PLoS pathogens · 2024Article
- CD44 receptor targeted nanoparticles augment immunity against tuberculosis in mice.Journal of controlled release : official journal of the Controlled Release Society · 2022Article
- Human Macrophages Exhibit GM-CSF Dependent Restriction ofFrontiers in immunology · 2022Article
- High Glucose Concentrations Impair the Processing and Presentation ofBiomolecules · 2021Article
- Human monocyte-derived macrophage responses to M. tuberculosis differ by the host's tuberculosis, diabetes or obesity status, and are enhanced by rapamycin.Tuberculosis (Edinburgh, Scotland) · 2021Article
- Article
- Rapid loss of early antigen-presenting activity of lymph node dendritic cells against Ag85A protein following Mycobacterium bovis BCG infection.BMC immunology · 2018Article
- Hyperglycaemia is inversely correlated with live M. bovis BCG-specific CD4Immunity, inflammation and disease · 2018Article
- Mycobacterium tuberculosis Molecular Determinants of Infection, Survival Strategies, and Vulnerable Targets.Pathogens (Basel, Switzerland) · 2018Review
- A Sex-Stratified Genome-Wide Association Study of Tuberculosis Using a Multi-Ethnic Genotyping Array.Frontiers in genetics · 2018Article
- Suboptimal Antigen Presentation Contributes to Virulence of Mycobacterium tuberculosis In Vivo.Journal of immunology (Baltimore, Md. : 1950) · 2016Article
- The role of 3-ketosteroid 1(2)-dehydrogenase in the pathogenicity of Mycobacterium tuberculosis.BMC microbiology · 2013Article
- Human phagosome processing of Mycobacterium tuberculosis antigens is modulated by interferon-γ and interleukin-10.Immunology · 2013Article
- The Tim3-galectin 9 pathway induces antibacterial activity in human macrophages infected with Mycobacterium tuberculosis.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- RNA-seq liver transcriptome analysis reveals an activated MHC-I pathway and an inhibited MHC-II pathway at the early stage of vaccine immunization in zebrafish.BMC genomics · 2012Article
- Crystal structure of Mycobacterium tuberculosis zinc-dependent metalloprotease-1 (Zmp1), a metalloprotease involved in pathogenicity.The Journal of biological chemistry · 2011Article
- Endoplasmic reticulum stress pathway-mediated apoptosis in macrophages contributes to the survival of Mycobacterium tuberculosis.PloS one · 2011Article
- Pathogenesis, immunology, and diagnosis of latent Mycobacterium tuberculosis infection.Clinical & developmental immunology · 2011Review
- Direct visualization of peptide/MHC complexes at the surface and in the intracellular compartments of cells infected in vivo by Leishmania major.PLoS pathogens · 2010Article
- The same well-characterized T cell epitope SIINFEKL expressed in the context of a cytoplasmic or secreted protein in BCG induces different CD8+ T cell responses.Immunology letters · 2010Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Mycobacterium tuberculosis resides in phagosomes inside macrophages. In this study, we analyzed the kinetics and location of M. tuberculosis peptide-major histocompatibility complex class II (MHC-II) complexes in M. tuberculosis-infected human macrophages. M. tuberculosis peptide-MHC-II complexes were detected with polyclonal autologous M. tuberculosis-specific CD4+ T cells or F9A6 T hybridoma cells specific for M. tuberculosis antigen (Ag) 85B (96-111). Macrophages processed heat-killed M. tuberculosis more rapidly and efficiently than live M. tuberculosis. To determine where M. tuberculosis peptide-MHC-II complexes were formed intracellularly, macrophages incubated with heat-killed M. tuberculosis were homogenized, and subcellular compartments were separated on Percoll density gradients analyzed with T cells. In THP-1 cells, M. tuberculosis Ag 85B (96- 111)-DR1 complexes appeared initially in phagosomes, followed by MHC class II compartment (MIIC) and the plasma membrane fractions. In monocyte-derived macrophages, M. tuberculosis peptide-MHC-II complexes appeared only in MIIC fractions and subsequently on the plasma membrane. Although phagosomes from both cell types acquired lysosome-associated membrane protein 1 (LAMP-1) and MHC-II, THP-1 phagosomes that support formation of M. tuberculosis peptide-MHC-II complexes had increased levels of both LAMP-1 and MHC-II. Thus, M. tuberculosis phagosomes with high levels of MHC-II and LAMP-1 and MIIC both have the potential to form peptide-MHC-II complexes from M. tuberculosis antigens in human macrophages.
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