Abstract
We examined nonopsonic binding of Mycobacterium avium-Mycobacterium intracellulare (MAI) by human leukocytes. Macrophages (M phi) avidly bound fluorescently labeled MAI in the absence of serum proteins. Binding appeared to be mediated by a lineage-specific, proteinaceous receptor on M phi, since (i) binding of labeled bacteria could be competitively inhibited by unlabeled MAI, (ii) treatment of M phi with trypsin ablated the ability of M phi to bind MAI, and (iii) the capacity to bind MAI was observed on monocytes, M phi, and stimulated polymorphonuclear cells but not on lymphocytes or unstimulated polymorphonuclear cells. The receptor for MAI appeared mobile in the plane of the membrane, since spreading of M phi on a carpet of immobilized, unlabeled MAI down modulated binding of labeled MAI added in suspension. The receptor required neither calcium nor magnesium for activity and appeared different from other known receptors for intracellular pathogens.
MeSH Terms
Binding Sites
Cell Membrane/drug effects,metabolism
Cells, Cultured
Humans
Kinetics
Leukocytes, Mononuclear/drug effects,metabolism
Macrophages/drug effects,metabolism
Mycobacterium avium Complex/metabolism
Neutrophils/drug effects,metabolism
T-Lymphocytes/drug effects,metabolism
Trypsin/pharmacology
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Catanzaro A
Department of Medicine, University of California, San Diego 92103.
Wright S D
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