TY - JOUR
T1 - Lectin-like attachment sites on murine pulmonary alveolar macrophages bind Aspergillus fumigatus conidia
AU - Kan, V. L.
AU - Bennett, J. E.
PY - 1988/1/1
Y1 - 1988/1/1
N2 - Murine pulmonary alveolar macrophages bound Aspergillus fumigatus conidia in vitro at 4 C and 37 C in the absence of serum or opsonins. This attachment was dependent on calcium and was sensitive to mild trypsinization and paraformaldehyde pretreatment of the macrophage membrane. Chitotriose, N-acetylglucosamine, D-mannose, α-methyl-mannoside, and L-fucose, but not D-galactose, were effective inhibitors of conidial binding. This pattern of reduction of conidial binding was consistent with that for the mannosyl-fucosyl receptor. In addition, conidial binding may be mediated by another lectin on the macrophage membrane, one that recognizes chitin components, because N-acetylglucosamine and chitotriose exhibited greater inhibition than expected for the mannosyl-fucosyl lectin.
AB - Murine pulmonary alveolar macrophages bound Aspergillus fumigatus conidia in vitro at 4 C and 37 C in the absence of serum or opsonins. This attachment was dependent on calcium and was sensitive to mild trypsinization and paraformaldehyde pretreatment of the macrophage membrane. Chitotriose, N-acetylglucosamine, D-mannose, α-methyl-mannoside, and L-fucose, but not D-galactose, were effective inhibitors of conidial binding. This pattern of reduction of conidial binding was consistent with that for the mannosyl-fucosyl receptor. In addition, conidial binding may be mediated by another lectin on the macrophage membrane, one that recognizes chitin components, because N-acetylglucosamine and chitotriose exhibited greater inhibition than expected for the mannosyl-fucosyl lectin.
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U2 - 10.1093/infdis/158.2.407
DO - 10.1093/infdis/158.2.407
M3 - Article
C2 - 3042877
AN - SCOPUS:0023733770
SN - 0022-1899
VL - 158
SP - 407
EP - 414
JO - Journal of Infectious Diseases
JF - Journal of Infectious Diseases
IS - 2
ER -