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J. Biol. Chem., Vol. 277, Issue 44, 41613-41623, November 1, 2002
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From the The in vitro binding of the
macrophage mannose receptor to a range of different bacterial
polysaccharides was investigated. The receptor was shown to bind to
purified capsular polysaccharides from Streptococcus
pneumoniae and to the lipopolysaccharides, but not capsular
polysaccharides, from Klebsiella pneumoniae. Binding was
Ca2+-dependent and inhibitable with
D-mannose. A fusion protein of the mannose receptor
containing carbohydrate recognition domains 4-7 and a full-length
soluble form of the mannose receptor containing all domains external to
the transmembrane region both displayed very similar binding
specificities toward bacterial polysaccharides, suggesting that domains
4-7 are sufficient for recognition of these structures. Surprisingly,
no direct correlation could be made between polysaccharide structure
and binding to the mannose receptor, suggesting that polysaccharide
conformation may play an important role in recognition. The full-length
soluble form of the mannose receptor was able to bind simultaneously
both polysaccharide via the carbohydrate recognition domains and
sulfated oligosaccharide via the cysteine-rich domain. The possible
involvement of the mannose receptor, either cell surface or soluble, in
the innate and adaptive immune responses to bacterial polysaccharides
is discussed.
Recognition of Bacterial Capsular Polysaccharides and
Lipopolysaccharides by the Macrophage Mannose Receptor*
§,,
Edward Jenner Institute for Vaccine
Research, Compton, Berkshire RG20 7NN, United Kingdom and the
¶ Sir William Dunn School of Pathology, University of Oxford,
South Parks Road, Oxford OX1 3RE, United Kingdom
*
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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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