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J. Biol. Chem., Vol. 277, Issue 23, 20379-20385, June 7, 2002
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From the Program in Cell Biology, Department of Medicine, National
Jewish Medical and Research Center, Denver, Colorado 80206
Increasing evidence now identifies surfactant
protein D (SP-D) as an important element of the innate immune system of
the lung. In this study, we examined the interactions of rat and human SP-D with the human pathogen, Mycoplasma pneumoniae. Rat
and human SP-D bound the organism with high affinity in a reaction that required Ca2+ and was inhibited by EGTA. Membranes derived
from the organism bound the proteins in a similar manner, except the
rat SP-D also exhibited a significant level of
Ca2+-independent binding. Pretreatment of membranes with
proteases did not alter the Ca2+-dependent SP-D
binding of membranes by either protein. Mannose, glucose, maltose, and
inositol, at millimolar concentrations, competed for human SP-D binding
to the bacterial membrane. Lipids extracted from membranes and
separated by two-dimensional thin layer chromatography bound human SP-D
with high affinity in a Ca2+-dependent
reaction. A tandem mutant of SP-D with E321Q and N323D substitutions,
failed to bind M. pneumoniae lipids, directly
implicating the carbohydrate recognition domain in the interaction. The
interaction of rat and human SP-D with M. pneumoniae was
unaffected by the presence of surfactant lipids and the hydrophobic
surfactant proteins. These findings demonstrate that M. pneumoniae is likely to be recognized by SP-D in the alveolar
environment and that primary determinants recognized on the organism
are lipid components of the cell membrane.
Human Surfactant Protein D (SP-D) Binds Mycoplasma
pneumoniae by High Affinity Interactions with Lipids*
*
This work was supported by National Institutes of Health
Grants HL 45286 and ALA-ARC 95.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Medicine,
National Jewish Medical Research Center, 1400 Jackson St., Denver, CO
80206. Tel.: 303-398-1300; Fax: 303-398-1806; E-mail: voelkerd@njc.org.
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