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Relationship between structures and biological activities of mycoplasmal diacylated lipopeptides and their recognition by Toll-like receptors 2 and 6

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Title: Relationship between structures and biological activities of mycoplasmal diacylated lipopeptides and their recognition by Toll-like receptors 2 and 6
Authors: Okusawa, Tsugumi Browse this author
Fujita, Mari Browse this author
Nakamura, Jun-ichiro Browse this author
Into, Takeshi Browse this author
Yasuda, Motoaki Browse this author
Yoshimura, Atsutoshi Browse this author
Hara, Yoshitaka Browse this author
Hasebe, Akira Browse this author
Golenbock, Douglas T. Browse this author
Morita, Manabu Browse this author
Kuroki, Yoshio Browse this author
Ogawa, Tomohiko Browse this author
Shibata, Ken-ichiro Browse this author →KAKEN DB
Keywords: Mycoplasma
diacylated lipopeptide
Toll-like receptor
Issue Date: Mar-2004
Publisher: American Society for Microbiology
Journal Title: Infection and immunity
Volume: 72
Issue: 3
Start Page: 1657
End Page: 1665
Publisher DOI: 10.1128/IAI.72.3.1657-1665.2004
PMID: 14977973
Abstract: The lipopeptide FSL-1 [S-(2,3-bispalmitoyloxypropyl)-Cys-Gly-Asp-Pro-Lys-His-Pro-Lys-Ser-Phe, Pam2CGDPKHPKSF] synthesized on the basis of the N-terminal structure of a Mycoplasma salivarium lipoprotein capable of activating normal human gingival fibroblasts to induce the cell surface expression of ICAM-1 revealed the activity to induce production of monocyte chemoattractant protein-1, IL-6 and IL-8. FSL-1 also activated macrophages to produce TNF-α as the M. fermentans-derived lipopeptide MALP-2 (Pam2CGNNDESNISFKEK), a potent macrophage-activating lipopeptide did. The level of the activity of FSL-1 was higher than that of MALP-2. This result suggests that the difference in the amino acid sequence of the peptide portion affects the activity, because the framework structure other than the amino acid sequence of the former is the same as that of the latter. To determine minimal structural requirements for the activity of FSL-1, the diacylglyceryl Cys and the peptideportions were examined for the activity. Both portions did not reveal the activity. A single amino acid substitution from Phe to Arg and a fatty acid substitution from palmitic acid to stearic acid drastically reduced the activity. The similar results were obtained by the NF-κB reporter activity of FSL-1 to human embryonic kidney (HEK) 293 cells transfected with Toll-like receptor 2 and 6 together with a NF-κB dependent luciferase reporter plasmid. These results suggest that both the diacylglyceryl and peptide portions of FSL-1 are indispensable for the expression of biological activities and for the recognition by Toll-like receptors 2 and 6, and that the recognition of FSL-1 by Toll-like receptors 2 and 6 appears to be hydrophobic.
Type: article (author version)
URI: http://hdl.handle.net/2115/43981
Appears in Collections:歯学院・歯学研究院 (Graduate School of Dental Medicine / Faculty of Dental Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 柴田 健一郎

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