Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry

Yukari Fujimoto, Katsunori Tanaka, Atsushi Shimoyama, Koichi Fukase

Research output: Book/ReportBook

5 Citations (Scopus)

Abstract

In this chapter, we describe synthetic studies on partial structures of lipopolysaccharide (LPS) and peptidoglycan (PGN), which work as tags for nonself recognition in innate immune system. Our previous studies demonstrated that lipid A is the endotoxic principle of LPS. The synthetic homogeneous preparations have enabled not only precise structure-activity relationships, but also recognition mechanisms of LPS with innate immune receptor complexes, including the TLR4/MD-2 complex, to be studied. Synthetic studies of lipid A and Kdo-lipid A from parasitic Helicobacter pylori revealed their low inflammatory activities, suggesting the molecular evolution to escape from the host immune system. A synthetic study of the partial structures of PGN has also contributed to the understanding of the innate immune mechanism. The biological activities of the synthetic fragments have revealed that the intracellular receptor Nod2 recognizes partial structures containing the muramyl dipeptide (MDP) moiety. The PGN of Gram-negative bacteria and some Gram-positive bacteria contain meso-diaminopimelic acid (meso-DAP), and recent studies have revealed that the intracellular receptor Nod1 recognizes DAP-containing peptides. We have synthesized DAP-containing PGN fragments, including the first chemical synthesis of tracheal cytotoxin (TCT). The ability of these fragments to stimulate human Nod1 as well as differences in Nod1 recognition for various synthesized ligand structures was elucidated. Cell-surface glycans such as N-glycans and O-glycans on glycoproteins and glycoconjugates work as signaling molecules for self-recognition and control immune system. Our new strategy using glycan-imaging in whole-body system is expected to unveil the dynamics of glycans in the body. Positron emission tomography (PET) is a noninvasive method that visualizes the locations and levels of radiotracer accumulation. We developed the facile labeling of peptides and proteins for PET imaging. The labeled glycoproteins and glycoclusters were then subjected to PET imaging in order to examine their in vivo dynamics, visualizing the differences in the circulatory residence of glycoproteins and glycoclusters in the presence or absence of sialic acid residues.

Original languageEnglish
PublisherUnknown Publisher
Number of pages20
Volume478
EditionC
DOIs
Publication statusPublished - 2010
Externally publishedYes

Publication series

NameMethods in Enzymology
No.C
Volume478
ISSN (Print)00766879

Fingerprint

Peptidoglycan
Polysaccharides
Animals
Lipid A
Positron emission tomography
Immune system
Positron-Emission Tomography
Lipopolysaccharides
Immune System
Glycoproteins
Imaging techniques
Bacteria
Acetylmuramyl-Alanyl-Isoglutamine
Diaminopimelic Acid
Whole Body Imaging
Peptides
Glycoconjugates
Molecular Evolution
Cytotoxins
Gram-Positive Bacteria

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Fujimoto, Y., Tanaka, K., Shimoyama, A., & Fukase, K. (2010). Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry. (C ed.) (Methods in Enzymology; Vol. 478, No. C). Unknown Publisher. https://doi.org/10.1016/S0076-6879(10)78016-2

Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry. / Fujimoto, Yukari; Tanaka, Katsunori; Shimoyama, Atsushi; Fukase, Koichi.

C ed. Unknown Publisher, 2010. 20 p. (Methods in Enzymology; Vol. 478, No. C).

Research output: Book/ReportBook

Fujimoto, Y, Tanaka, K, Shimoyama, A & Fukase, K 2010, Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry. Methods in Enzymology, no. C, vol. 478, vol. 478, C edn, Unknown Publisher. https://doi.org/10.1016/S0076-6879(10)78016-2
Fujimoto Y, Tanaka K, Shimoyama A, Fukase K. Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry. C ed. Unknown Publisher, 2010. 20 p. (Methods in Enzymology; C). https://doi.org/10.1016/S0076-6879(10)78016-2
Fujimoto, Yukari ; Tanaka, Katsunori ; Shimoyama, Atsushi ; Fukase, Koichi. / Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry. C ed. Unknown Publisher, 2010. 20 p. (Methods in Enzymology; C).
@book{1efe4a41781a4b6da0868b3a4dfbf1c4,
title = "Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry",
abstract = "In this chapter, we describe synthetic studies on partial structures of lipopolysaccharide (LPS) and peptidoglycan (PGN), which work as tags for nonself recognition in innate immune system. Our previous studies demonstrated that lipid A is the endotoxic principle of LPS. The synthetic homogeneous preparations have enabled not only precise structure-activity relationships, but also recognition mechanisms of LPS with innate immune receptor complexes, including the TLR4/MD-2 complex, to be studied. Synthetic studies of lipid A and Kdo-lipid A from parasitic Helicobacter pylori revealed their low inflammatory activities, suggesting the molecular evolution to escape from the host immune system. A synthetic study of the partial structures of PGN has also contributed to the understanding of the innate immune mechanism. The biological activities of the synthetic fragments have revealed that the intracellular receptor Nod2 recognizes partial structures containing the muramyl dipeptide (MDP) moiety. The PGN of Gram-negative bacteria and some Gram-positive bacteria contain meso-diaminopimelic acid (meso-DAP), and recent studies have revealed that the intracellular receptor Nod1 recognizes DAP-containing peptides. We have synthesized DAP-containing PGN fragments, including the first chemical synthesis of tracheal cytotoxin (TCT). The ability of these fragments to stimulate human Nod1 as well as differences in Nod1 recognition for various synthesized ligand structures was elucidated. Cell-surface glycans such as N-glycans and O-glycans on glycoproteins and glycoconjugates work as signaling molecules for self-recognition and control immune system. Our new strategy using glycan-imaging in whole-body system is expected to unveil the dynamics of glycans in the body. Positron emission tomography (PET) is a noninvasive method that visualizes the locations and levels of radiotracer accumulation. We developed the facile labeling of peptides and proteins for PET imaging. The labeled glycoproteins and glycoclusters were then subjected to PET imaging in order to examine their in vivo dynamics, visualizing the differences in the circulatory residence of glycoproteins and glycoclusters in the presence or absence of sialic acid residues.",
author = "Yukari Fujimoto and Katsunori Tanaka and Atsushi Shimoyama and Koichi Fukase",
year = "2010",
doi = "10.1016/S0076-6879(10)78016-2",
language = "English",
volume = "478",
series = "Methods in Enzymology",
publisher = "Unknown Publisher",
number = "C",
edition = "C",

}

TY - BOOK

T1 - Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry

AU - Fujimoto, Yukari

AU - Tanaka, Katsunori

AU - Shimoyama, Atsushi

AU - Fukase, Koichi

PY - 2010

Y1 - 2010

N2 - In this chapter, we describe synthetic studies on partial structures of lipopolysaccharide (LPS) and peptidoglycan (PGN), which work as tags for nonself recognition in innate immune system. Our previous studies demonstrated that lipid A is the endotoxic principle of LPS. The synthetic homogeneous preparations have enabled not only precise structure-activity relationships, but also recognition mechanisms of LPS with innate immune receptor complexes, including the TLR4/MD-2 complex, to be studied. Synthetic studies of lipid A and Kdo-lipid A from parasitic Helicobacter pylori revealed their low inflammatory activities, suggesting the molecular evolution to escape from the host immune system. A synthetic study of the partial structures of PGN has also contributed to the understanding of the innate immune mechanism. The biological activities of the synthetic fragments have revealed that the intracellular receptor Nod2 recognizes partial structures containing the muramyl dipeptide (MDP) moiety. The PGN of Gram-negative bacteria and some Gram-positive bacteria contain meso-diaminopimelic acid (meso-DAP), and recent studies have revealed that the intracellular receptor Nod1 recognizes DAP-containing peptides. We have synthesized DAP-containing PGN fragments, including the first chemical synthesis of tracheal cytotoxin (TCT). The ability of these fragments to stimulate human Nod1 as well as differences in Nod1 recognition for various synthesized ligand structures was elucidated. Cell-surface glycans such as N-glycans and O-glycans on glycoproteins and glycoconjugates work as signaling molecules for self-recognition and control immune system. Our new strategy using glycan-imaging in whole-body system is expected to unveil the dynamics of glycans in the body. Positron emission tomography (PET) is a noninvasive method that visualizes the locations and levels of radiotracer accumulation. We developed the facile labeling of peptides and proteins for PET imaging. The labeled glycoproteins and glycoclusters were then subjected to PET imaging in order to examine their in vivo dynamics, visualizing the differences in the circulatory residence of glycoproteins and glycoclusters in the presence or absence of sialic acid residues.

AB - In this chapter, we describe synthetic studies on partial structures of lipopolysaccharide (LPS) and peptidoglycan (PGN), which work as tags for nonself recognition in innate immune system. Our previous studies demonstrated that lipid A is the endotoxic principle of LPS. The synthetic homogeneous preparations have enabled not only precise structure-activity relationships, but also recognition mechanisms of LPS with innate immune receptor complexes, including the TLR4/MD-2 complex, to be studied. Synthetic studies of lipid A and Kdo-lipid A from parasitic Helicobacter pylori revealed their low inflammatory activities, suggesting the molecular evolution to escape from the host immune system. A synthetic study of the partial structures of PGN has also contributed to the understanding of the innate immune mechanism. The biological activities of the synthetic fragments have revealed that the intracellular receptor Nod2 recognizes partial structures containing the muramyl dipeptide (MDP) moiety. The PGN of Gram-negative bacteria and some Gram-positive bacteria contain meso-diaminopimelic acid (meso-DAP), and recent studies have revealed that the intracellular receptor Nod1 recognizes DAP-containing peptides. We have synthesized DAP-containing PGN fragments, including the first chemical synthesis of tracheal cytotoxin (TCT). The ability of these fragments to stimulate human Nod1 as well as differences in Nod1 recognition for various synthesized ligand structures was elucidated. Cell-surface glycans such as N-glycans and O-glycans on glycoproteins and glycoconjugates work as signaling molecules for self-recognition and control immune system. Our new strategy using glycan-imaging in whole-body system is expected to unveil the dynamics of glycans in the body. Positron emission tomography (PET) is a noninvasive method that visualizes the locations and levels of radiotracer accumulation. We developed the facile labeling of peptides and proteins for PET imaging. The labeled glycoproteins and glycoclusters were then subjected to PET imaging in order to examine their in vivo dynamics, visualizing the differences in the circulatory residence of glycoproteins and glycoclusters in the presence or absence of sialic acid residues.

UR - http://www.scopus.com/inward/record.url?scp=77956294598&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=77956294598&partnerID=8YFLogxK

U2 - 10.1016/S0076-6879(10)78016-2

DO - 10.1016/S0076-6879(10)78016-2

M3 - Book

C2 - 20816488

AN - SCOPUS:77956294598

VL - 478

T3 - Methods in Enzymology

BT - Self and nonself recognition with bacterial and animal glycans, surveys by synthetic chemistry

PB - Unknown Publisher

ER -