M D Melo1, R W Stokes. 1. Department of Pathology and Laboratory Medicine, University of British Columbia, Canada.
Abstract
UNLABELLED: We are interested in identifying a suitable model for investigating mycobacteria interactions with alveolar macrophages. MH-S, a murine alveolar macrophage cell line, is a possible candidate. OBJECTIVE: To compare the receptor mediated interactions of mycobacteria with primary murine macrophages and MH-S. DESIGN: The association of MH-S monolayers with Mycobacterium tuberculosis (MTB) and other defined particles was compared to that of resident Day 1 peritoneal macrophage (PM) and Day 4 alveolar macrophage (AM) monolayers. RESULTS: In the absence of serum, the association of MTB with MH-S was comparable to that of AM, with approximately 35% of each macrophage type binding at least one bacterium. In contrast, almost 80% of PM bound at least one bacterium. MTB binding was enhanced for all macrophage types by a heat-labile component of normal mouse serum. Antibodies recognising CR3 inhibited the serum-mediated enhanced binding of MTB by MH-S. Binding of latex, immunoglobulin coated or complement coated SRBC by MH-S, AM and PM was comparable. Binding of zymosan by MH-S was greatly inferior to AM and PM. CONCLUSION: The receptor expression and particle binding properties of MH-S are similar to AM in many, but not all, ways. MH-S, therefore, has the potential to be used as a model for investigating MTB-macrophage interactions.
UNLABELLED: We are interested in identifying a suitable model for investigating mycobacteria interactions with alveolar macrophages. MH-S, a murine alveolar macrophage cell line, is a possible candidate. OBJECTIVE: To compare the receptor mediated interactions of mycobacteria with primary murine macrophages and MH-S. DESIGN: The association of MH-S monolayers with Mycobacterium tuberculosis (MTB) and other defined particles was compared to that of resident Day 1 peritoneal macrophage (PM) and Day 4 alveolar macrophage (AM) monolayers. RESULTS: In the absence of serum, the association of MTB with MH-S was comparable to that of AM, with approximately 35% of each macrophage type binding at least one bacterium. In contrast, almost 80% of PM bound at least one bacterium. MTB binding was enhanced for all macrophage types by a heat-labile component of normal mouse serum. Antibodies recognising CR3 inhibited the serum-mediated enhanced binding of MTB by MH-S. Binding of latex, immunoglobulin coated or complement coated SRBC by MH-S, AM and PM was comparable. Binding of zymosan by MH-S was greatly inferior to AM and PM. CONCLUSION: The receptor expression and particle binding properties of MH-S are similar to AM in many, but not all, ways. MH-S, therefore, has the potential to be used as a model for investigating MTB-macrophage interactions.
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