Profiling Carbohydrate-Receptor Interaction with Recombinant Innate Immunity Receptor-Fc Fusion Proteins*
Identifieur interne : 000700 ( Pmc/Corpus ); précédent : 000699; suivant : 000701Profiling Carbohydrate-Receptor Interaction with Recombinant Innate Immunity Receptor-Fc Fusion Proteins*
Auteurs : Tsui-Ling Hsu ; Shih-Chin Cheng ; Wen-Bin Yang ; See-Wen Chin ; Bo-Hua Chen ; Ming-Ting Huang ; Shie-Liang Hsieh ; Chi-Huey WongSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2009.
Abstract
The recognition of bacteria, viruses, fungi, and other microbes is controlled by host immune cells, which are equipped with many innate immunity receptors, such as Toll-like receptors, C-type lectin receptors, and immunoglobulin-like receptors. Our studies indicate that the immune modulating properties of many herbal drugs, for instance, the medicinal fungus Reishi (
Url:
DOI: 10.1074/jbc.M109.065961
PubMed: 19837675
PubMed Central: 2787309
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PMC:2787309Le document en format XML
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<author><name sortKey="Yang, Wen Bin" sort="Yang, Wen Bin" uniqKey="Yang W" first="Wen-Bin" last="Yang">Wen-Bin Yang</name>
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<author><name sortKey="Huang, Ming Ting" sort="Huang, Ming Ting" uniqKey="Huang M" first="Ming-Ting" last="Huang">Ming-Ting Huang</name>
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<author><name sortKey="Hsieh, Shie Liang" sort="Hsieh, Shie Liang" uniqKey="Hsieh S" first="Shie-Liang" last="Hsieh">Shie-Liang Hsieh</name>
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<series><title level="j">The Journal of Biological Chemistry</title>
<idno type="ISSN">0021-9258</idno>
<idno type="eISSN">1083-351X</idno>
<imprint><date when="2009">2009</date>
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<front><div type="abstract" xml:lang="en"><p>The recognition of bacteria, viruses, fungi, and other microbes is controlled by host immune cells, which are equipped with many innate immunity receptors, such as Toll-like receptors, C-type lectin receptors, and immunoglobulin-like receptors. Our studies indicate that the immune modulating properties of many herbal drugs, for instance, the medicinal fungus Reishi (<italic>Ganoderma lucidum</italic>
) and <italic>Cordyceps sinensis</italic>
, could be attributed to their polysaccharide components. These polysaccharides specifically interact with and activate surface receptors involved in innate immunity. However, due to the complexity of polysaccharides and their various sources from medicinal fungi, quantitative analysis of medicinal polysaccharide extracts with regard to their functions represents a major challenge. To profile carbohydrate-immune receptor interactions, the extracellular domains of 17 receptors were cloned as Fc-fusion proteins, such that their interactions with immobilized polysaccharides could be probed in an enzyme-linked immunosorbent assay. The results show that several innate immune receptors, including Dectin-1, DC-SIGN, Langerin, Kupffer cell receptor, macrophage mannose receptor, TLR2, and TLR4, interact with the polysaccharide extracts from <italic>G. lucidum</italic>
(GLPS). This analysis revealed distinct polysaccharide profiles from different sources of medicinal fungi, and the innate immune receptor-based enzyme-linked immunosorbent assay described here can serve as a high-throughput profiling method for the characterization and quality control of medicinal polysaccharides. It also provides a means to dissect the molecular mechanism of medicinal polysaccharide-induced immunomodulation events.</p>
</div>
</front>
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<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id>
<journal-id journal-id-type="hwp">jbc</journal-id>
<journal-id journal-id-type="pmc">jbc</journal-id>
<journal-id journal-id-type="publisher-id">JBC</journal-id>
<journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title>
</journal-title-group>
<issn pub-type="ppub">0021-9258</issn>
<issn pub-type="epub">1083-351X</issn>
<publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name>
<publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">19837675</article-id>
<article-id pub-id-type="pmc">2787309</article-id>
<article-id pub-id-type="publisher-id">M109.065961</article-id>
<article-id pub-id-type="doi">10.1074/jbc.M109.065961</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Glycobiology and Extracellular Matrices</subject>
</subj-group>
</article-categories>
<title-group><article-title>Profiling Carbohydrate-Receptor Interaction with Recombinant Innate Immunity Receptor-Fc Fusion Proteins<xref ref-type="fn" rid="FN1">*</xref>
<xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic>
</sup>
</xref>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Hsu</surname>
<given-names>Tsui-Ling</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cheng</surname>
<given-names>Shih-Chin</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Yang</surname>
<given-names>Wen-Bin</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Chin</surname>
<given-names>See-Wen</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Chen</surname>
<given-names>Bo-Hua</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Huang</surname>
<given-names>Ming-Ting</given-names>
</name>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Hsieh</surname>
<given-names>Shie-Liang</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="aff" rid="aff2"><sup>§</sup>
</xref>
<xref ref-type="aff" rid="aff3"><sup>¶</sup>
</xref>
<xref ref-type="corresp" rid="cor1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wong</surname>
<given-names>Chi-Huey</given-names>
</name>
<xref ref-type="aff" rid="aff1"><sup>‡</sup>
</xref>
<xref ref-type="aff" rid="aff4"><sup>‖</sup>
</xref>
<xref ref-type="corresp" rid="cor2"><sup>2</sup>
</xref>
</contrib>
<aff id="aff1">From the<label>‡</label>
The Genomics Research Center, Academia Sinica, Taipei 115,</aff>
<aff id="aff2">the<label>§</label>
Institute of Microbiology and Immunology, National Yang-Ming University, Taipei 112, and</aff>
<aff id="aff3">the<label>¶</label>
Immunology Research Center, Taipei Veterans General Hospital, Taipei 112, Taiwan and</aff>
<aff id="aff4">the<label>‖</label>
Department of Chemistry and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037</aff>
</contrib-group>
<author-notes><corresp id="cor1"><label>1</label>
To whom correspondence may be addressed: <addr-line>Institute of Microbiology and Immunology, National Yang-Ming University, 155 Li-Nong St., Section 2, Taipei 112, Taiwan.</addr-line>
Tel.: <phone>886-2-28267161</phone>
; Fax: <fax>886-2-28277933</fax>
; E-mail: <email>slhsieh@ym.edu.tw</email>
.</corresp>
<corresp id="cor2"><label>2</label>
To whom correspondence may be addressed: <addr-line>The Genomics Research Center, Academia Sinica, 128 Academia Rd., Section 2, Taipei 115, Taiwan.</addr-line>
Tel.: <phone>886-2-27899400</phone>
; Fax: <fax>886-2-27853852</fax>
; E-mail: <email>chwong@gate.sinica.edu.tw</email>
.</corresp>
</author-notes>
<pub-date pub-type="ppub"><day>11</day>
<month>12</month>
<year>2009</year>
</pub-date>
<pub-date pub-type="epub"><day>16</day>
<month>10</month>
<year>2009</year>
</pub-date>
<volume>284</volume>
<issue>50</issue>
<fpage>34479</fpage>
<lpage>34489</lpage>
<history><date date-type="received"><day>14</day>
<month>9</month>
<year>2009</year>
</date>
</history>
<permissions><copyright-statement>© 2009 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement>
</permissions>
<self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc05009034479.pdf"></self-uri>
<abstract><p>The recognition of bacteria, viruses, fungi, and other microbes is controlled by host immune cells, which are equipped with many innate immunity receptors, such as Toll-like receptors, C-type lectin receptors, and immunoglobulin-like receptors. Our studies indicate that the immune modulating properties of many herbal drugs, for instance, the medicinal fungus Reishi (<italic>Ganoderma lucidum</italic>
) and <italic>Cordyceps sinensis</italic>
, could be attributed to their polysaccharide components. These polysaccharides specifically interact with and activate surface receptors involved in innate immunity. However, due to the complexity of polysaccharides and their various sources from medicinal fungi, quantitative analysis of medicinal polysaccharide extracts with regard to their functions represents a major challenge. To profile carbohydrate-immune receptor interactions, the extracellular domains of 17 receptors were cloned as Fc-fusion proteins, such that their interactions with immobilized polysaccharides could be probed in an enzyme-linked immunosorbent assay. The results show that several innate immune receptors, including Dectin-1, DC-SIGN, Langerin, Kupffer cell receptor, macrophage mannose receptor, TLR2, and TLR4, interact with the polysaccharide extracts from <italic>G. lucidum</italic>
(GLPS). This analysis revealed distinct polysaccharide profiles from different sources of medicinal fungi, and the innate immune receptor-based enzyme-linked immunosorbent assay described here can serve as a high-throughput profiling method for the characterization and quality control of medicinal polysaccharides. It also provides a means to dissect the molecular mechanism of medicinal polysaccharide-induced immunomodulation events.</p>
</abstract>
<funding-group><award-group><funding-source id="CS100">National Institutes of Health</funding-source>
<award-id rid="CS100">GM62116</award-id>
</award-group>
</funding-group>
</article-meta>
</front>
</pmc>
</record>
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