A role of the Ca2+ binding site of DC-SIGN in the phagocytosis of E. coli.
HEK293 cells stably expressing DC-SIGN (293/DC-SIGN) were examined for phagocytosis of Escherichia coli. 293/DC-SIGN stable transfectants were able to mediate phagocytosis of E. coli. The phagocytosis was inhibited by EDTA or several inhibitors specific for Syk kinase, Raf kinase and the transcription factor NF-kappaB. DC-SIGN consists of characteristic domains and motifs such as CRD, neck, incomplete ITAM, dileucine and tri-acidic cluster. HEK293 cells expressing mutants of DC-SIGN were also examined for the phagocytosis. It was found that Ca(2+) binding sites in the CRD of DC-SIGN were involved in phagocytosis of bacteria as well as multimerization of DC-SIGN, and the neck region played a role in efficiency of binding to microbes as well as multimerization of the protein.
Iyori
Mitsuhiro
M
Division of Oral Molecular Microbiology, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan; Division of Research Fellow of the Japan Society for the Promotion of Science, Japan.
Ohtani
Makoto
M
Division of Oral Molecular Microbiology, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan; Division of Oral and Maxillofacial Surgery, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan.
Hasebe
Akira
A
Division of Oral Molecular Microbiology, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan.
Totsuka
Yasunori
Y
Division of Oral and Maxillofacial Surgery, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan.
Shibata
Ken-Ichiro
KI
Division of Oral Molecular Microbiology, Department of Oral Pathobiological Science, Hokkaido University Graduate School of Dental Medicine, Nishi 7, Kita 13, Kita-Ku, Sapporo 060-8586, Japan. Electronic address: shibaken@den.hokudai.ac.jp.
D001665:Binding Sites; D002118:Calcium / Q000378:metabolism*; D015815:Cell Adhesion Molecules / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004492:Edetic Acid / Q000494:pharmacology; D004926:Escherichia coli / Q000276:immunology*; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases / Q000378:metabolism; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D037181:Lectins, C-Type / Q000235:genetics / Q000378:metabolism*; D016328:NF-kappa B / Q000037:antagonists & inhibitors / Q000378:metabolism; D010587:Phagocytosis / Q000187:drug effects / Q000235:genetics; D017434:Protein Structure, Tertiary; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism; D000072377:Syk Kinase; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin
D002118:Calcium; D015815:Cell Adhesion Molecules; D004492:Edetic Acid; D056572:Histone Deacetylase Inhibitors; D006655:Histone Deacetylases; D047908:Intracellular Signaling Peptides and Proteins; D037181:Lectins, C-Type; D016328:NF-kappa B; D011505:Protein-Tyrosine Kinases; D011956:Receptors, Cell Surface; D029701:Saccharomyces cerevisiae Proteins; D000072377:Syk Kinase; D000099215:DC-Specific ICAM-3 Grabbing Nonintegrin; C000606896:SYK protein, human; C507989:Raf60 protein, S cerevisiae