TY - JOUR
T1 - Mycobacterium avium-M. intracellulare binds to the integrin receptor α(V)β3 on human monocytes and monocyte-derived macrophages
AU - Rao, S. P.
AU - Ogata, K.
AU - Catanzaro, A.
PY - 1993
Y1 - 1993
N2 - Mycobacterium avium-M. intracellulare is an intracellular pathogen responsible for the highest incidence of disseminated bacterial infection in patients with AIDS. Treatment of the infection is difficult and has been of limited efficacy. Attachment of the organism to macrophages is a critical early step in the establishment of the disease. In the present study, we isolated and identified a receptor that mediates attachment of M. avium-M. intracellulare to human peripheral blood monocytes and monocyte-derived macrophages. On Western blotting, (immunoblotting), the receptor was found to cross-react with antibodies against a human vitronectin receptor (α(V)β3). The receptor could be purified from monocyte extracts by using monoclonal antibodies (MAbs) against the α(V) subunit of vitronectin receptor coupled to CNBr-Sepharose 4B, as well as with the adhesive tripeptide sequence arginine-glycine-aspartic acid (RGD) coupled to CNBr-Sepharose 4B. Surface- bound MAbs directed against α(V)β3 were found to inhibit the attachment of M. avium-M. intracellulare to monocyte-derived macrophages in an in vitro inhibition assay, while MAbs directed against CD14, CD18, α2β1 and platelet glycoprotein gpIIb/IIIa receptors did not inhibit this attachment. These observations suggest that α(V)β3 on the surface of human monocytes and monocyte-derived macrophages may function as a receptor for M. avium-M. intracellulare. Identification of a receptor for M. avium-M. intracellulare on macrophages may offer new approaches to the prevention and control of M. avium-M. intracellulare infection at the cellular level.
AB - Mycobacterium avium-M. intracellulare is an intracellular pathogen responsible for the highest incidence of disseminated bacterial infection in patients with AIDS. Treatment of the infection is difficult and has been of limited efficacy. Attachment of the organism to macrophages is a critical early step in the establishment of the disease. In the present study, we isolated and identified a receptor that mediates attachment of M. avium-M. intracellulare to human peripheral blood monocytes and monocyte-derived macrophages. On Western blotting, (immunoblotting), the receptor was found to cross-react with antibodies against a human vitronectin receptor (α(V)β3). The receptor could be purified from monocyte extracts by using monoclonal antibodies (MAbs) against the α(V) subunit of vitronectin receptor coupled to CNBr-Sepharose 4B, as well as with the adhesive tripeptide sequence arginine-glycine-aspartic acid (RGD) coupled to CNBr-Sepharose 4B. Surface- bound MAbs directed against α(V)β3 were found to inhibit the attachment of M. avium-M. intracellulare to monocyte-derived macrophages in an in vitro inhibition assay, while MAbs directed against CD14, CD18, α2β1 and platelet glycoprotein gpIIb/IIIa receptors did not inhibit this attachment. These observations suggest that α(V)β3 on the surface of human monocytes and monocyte-derived macrophages may function as a receptor for M. avium-M. intracellulare. Identification of a receptor for M. avium-M. intracellulare on macrophages may offer new approaches to the prevention and control of M. avium-M. intracellulare infection at the cellular level.
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M3 - Article
C2 - 7678588
AN - SCOPUS:0027398524
SN - 0019-9567
VL - 61
SP - 663
EP - 670
JO - Infection and immunity
JF - Infection and immunity
IS - 2
ER -