Mycobacterium tuberculosis heparin-binding haemagglutinin adhesin (HBHA) triggers receptor-mediated transcytosis without altering the integrity of tight junctions

Autor: Delphine Cayet, Anne-Sophie Debrie, Franco D. Menozzi, Roméo Cecchelli, Marie-Pierre Dehouck, Dominique Raze, Venkata M. Reddy, Camille Locht
Přispěvatelé: Infections et inflammation : Pathogenèse et prévention, Institut Pasteur de Lille, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université de Lille, Droit et Santé, Mécanismes moléculaires de la pathogenèse bactérienne, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP)-Institut National de la Santé et de la Recherche Médicale (INSERM), University of Illinois College of Medicine, University of Illinois System, Laboratoire de Physiopathologie de la Barrière Hémato-Encéphalique (LBHE), Université d'Artois (UA), Mécanismes moléculaires de la pathogénie microbienne, This research was supported by Inserm, Institut Pasteur de Lille, Ministère de la Recherche et de la Technologie, and Université d'Artois., We thank Maria Cristina Vidal-Pessolani and Alice Miranda (Instituto Oswaldo Cruz, Rio de Janeiro) for critical reading of the manuscript.
Rok vydání: 2004
Předmět:
Endocytic cycle
MESH: Proteoglycans/metabolism
Dissemination
Cell junction
chemistry.chemical_compound
MESH: Biological Transport/drug effects
Lectins
MESH: Animals
Transcellular
Cytoskeleton
0303 health sciences
Tight junction
MESH: Neuroglia/metabolism
MESH: Tight Junctions/drug effects
Heparan sulfate
Endocytosis
3. Good health
Cell biology
MESH: Cattle
MESH: Epithelial Cells/metabolism
Infectious Diseases
MESH: Mycobacterium tuberculosis
Transcytosis
MESH: Receptors
Cell Surface/metabolism
Proteoglycans
Neuroglia
MESH: Rats
Immunology
MESH: Epithelial Cells/ultrastructure
Receptors
Cell Surface
Biology
Microbiology
MESH: Cytoskeleton/metabolism
HBHA
Cell Line
Tight Junctions
03 medical and health sciences
MESH: Tight Junctions/physiology
Tuberculosis
Animals
Humans
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Transport Vesicles
030304 developmental biology
MESH: Endocytosis/drug effects
MESH: Humans
030306 microbiology
MESH: Actins/metabolism
Biological Transport
Epithelial Cells
Receptor-mediated endocytosis
Mycobacterium tuberculosis
MESH: Lectins/pharmacology
Actins
MESH: Cell Line
Rats
chemistry
Cattle
MESH: Transport Vesicles/metabolism
Zdroj: Microbes and Infection
Microbes and Infection, Elsevier, 2006, 8 (1), pp.1-9. ⟨10.1016/j.micinf.2005.03.023⟩
ISSN: 1286-4579
DOI: 10.1016/j.micinf.2005.03.023⟩
Popis: International audience; Mycobacterium tuberculosis, the etiologic agent of tuberculosis, adheres to, invades and multiplies in both professional phagocytes and epithelial cells. Adherence to epithelial cells is predominantly mediated by the 28-kDa heparin-binding haemagglutinin adhesin (HBHA), which is also required for the extrapulmonary dissemination of the bacilli. To study the cellular mechanisms that might result in HBHAmediated extrapulmonary dissemination, we used a transwell model of cellular barrier and fluorescence microscopy and found that HBHA induces a reorganization of the actin filament network in confluent endothelial cells, but does not affect the tight junctions that link them. When coupled to colloidal gold particles, HBHA-mediated a rapid attachment of the particles to the membrane of human laryngeal epithelial cells (non polarized HEp-2 cells) and human type II pneumocytes (polarized A-549 pneumocytes). After attachment, the particles were internalized in membrane-bound vacuoles that migrated across the polarized pneumocytes to reach the basal side. Attachment of the HBHAcoated particles was not observed when the epithelial cells were pretreated with heparinase III, a lyase that specifically cleaves the heparan sulfate chains borne by the proteoglycans. Furthermore, no binding was observed when the gold particles were coated with HBHA lacking its C-terminal heparin-binding domain. These observations indicate that HBHA induces receptor-mediated endocytosis through the recognition of heparan sulfate-containing proteoglycans by the heparin-binding domain of the adhesin. In addition, the transcellular migration of the endocytic vacuoles containing HBHA-coated particles suggests that HBHA induces epithelial transcytosis, which may represent amacrophageindependent extrapulmonary dissemination mechanism leading to systemic infection by M. tuberculosis.
Databáze: OpenAIRE
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