The Nakanishi Symposium
on Natural Products & Bioorganic Chemistry

Doshisha University
March 24, 2016

Sponsored by
The Chemical Society of Japan&
The American Chemical Society

— Table of Contents ―Profile of Dr. Shoichi Kusumoto;Prize Winner of the Nakanishi Prize 2016
Program of the Award Ceremonyof the Nakanishi Prize & Nakanishi Symposium

…… 2
…… 4

“Microbial Immunomodulatory Glycoconjugates;
Syntheses and Biological Functions”…… 5

Prof. Yukari Fujimoto (Keio University)“Nucleic Acid Sensing by Toll-like Receptors”
Prof. Kensuke Miyake (The Univ. of Tokyo）…… 6“Identification of a Novel Glycolipid Essential
for Membrane Protein Integration”
Dr. Keiko Shimamoto (Suntory Foundation for…… 7Life Sciences）“Quest for Synthetic Chemistry’s Initiative in…… 10

Glycobiology”
Prof. Yukishige Ito (RIKEN)Award Lecture“Chemistry and Biological Functions of
Bacterial Cell Surface Glycoconjugates”
Dr. Shoichi Kusumoto(Professor Emeritus, Osaka University)

－1－

…… 12

Kusumoto, Shoichi
Professor Emeritus, Osaka University■EDUCATION
B.Sc. Chemistry, Faculty of Science, Osaka University
Ph. D. Organic Chemistry, Osaka University

1963
1969

■ACADEMIC CAREER
Osaka City University
1964 – 1969, 1971 - 1972
Research Associate, Inst. of Organic Chemistry, Faculty of Science
German Cancer Research Center, Heidelberg
1969 - 1971
Research Fellow of Alexander von Humboldt-Foundation
Osaka University
1972 - 2004
Department of Chemistry, Graduate School of Science
Research Associate, Associate Professor, then Professor of Organic
Chemistry
Suntory Institute for Bioorganic Research
2004 - 2011
Research Director－2－

■RESEARCH TOPICS
 Synthesis of immunostimulatory bacterial peptidoglycan partial
structures
 Structure, synthesis and biological functions of bacterial
endotoxin
 Synthetic strategies for glycoconjugates: versatile protecting
groups and efficient glycosylation■SELECTED PUBLICATIONS
1. Key structures of bacterial peptidoglycan and lipopolysaccharide
triggering the innate immune system of higher animals: Chemical
synthesis and functional studies. S. Kusumoto, K. Fukase, T. Shiba,Proc. Japan Acad. Ser. B, 2010, 86 (4), 322-337.
2. Synthesis of endotoxic principle of bacterial lipopolysaccharide
and its recognition by the innate immune systems of hosts. S.
Kusumoto, K. Fukase, Chem. Rec., 2006; 6:333-343.
3. Synthesis of Lipopolysaccharide, Peptidoglycan, and Lipoteichoic
Acid Fragments. S. Kusumoto, K. Fukase, Y. Fujimoto,“Comprehensive Glycosicience”, Vol. 1, Ed J.P. Kammeling,
Elsevier (Amsterdam 2007), pp. 685-711.
4. Synthesis of glycolipids. S. Kusumoto, M. Oikawa, “Glycoscience
III”, eds. B. F-Reid, K. Tatsuta, and J. Thiem, Springer (Berlin,2001), pp. 2107-2148.
■AWARDS Award of the International Society of Immunopharmacology 1983
 Award of the Chemical Society of Japan1999
 Bang Award of the International Society of Endotoxin
and Innate Immunity
2004

－3－

Nakanishi Symposium 2016
Organized by：Nakanishi Symposium Organizing Committee
Co-organized by: Chemical Society of Japan,
Division of Natural Products Chemistry & Biological Science

Date
Venue

March 24th, 2016, 13:30–17:30
Doshisha University(3F 301, Keido-kan Bldg., Kyotanabe Campus)

Program■13:30-14:00
Award Ceremony of Nakanishi Prize 2016
Presider Prof. Michio Murata (Osaka University)
Prize Winner of the Nakanishi Prize 2016:
Dr. Shoichi Kusumoto; Professor Emeritus of Osaka University■14:00-17:00
Nakanishi Symposium
Presider Prof. Minoru Ueda (Tohoku University)
14:00- “Microbial Immunomodulatory Glycoconjugates;
Syntheses and Biological Functions”
Prof. Yukari Fujimoto: (Keio University)
14:30- “Nucleic Acid Sensing by Toll-like Receptors”
Prof. Kensuke Miyake (The University of Tokyo)
Presider Prof. Keisuke Suzuki (Tokyo Institute of Technology)
15:00- “Identification of a Novel Glycolipid Essential for
Membrane Protein Integration”
Dr. Keiko Shimamoto (Suntory Foundation for Life Sciences）
15:30- “Quest for Synthetic Chemistry’s Initiative in Glycobiology”
Prof. Yukishige Ito (RIKEN)
16:00-16:10 ---Break--Presider Prof. Michio Murata; Osaka University
16:10- Award Lecture “Chemistry and Biological Functions of
Bacterial Cell Surface Glycoconjugates”
Dr. Shoichi Kusumoto■17:10- Closing Remarks－4－Microbial Immunomodulatory Glycoconjugates;
Syntheses and Biological Functions
Yukari Fujimoto
Department of Chemistry, Faculty of Science and Technology,
Keio University
fujimotoy@chem.keio.ac.jp

Microbial surface glyco- and lipid-conjugates often show
immunomodulatory activities, and some of these compounds arerecognized by the innate immune receptors, such as TLRs, NLRs,
RLRs and CLRs, to trigger the immune system. The representative
ligands include bacterial lipopolysaccharide (LPS)/lipid A,
peptidoglycan (PGN), and lipo peptides.
PGN is a component of bacterial cell wall consisting of long glycans
having alternating GlcNAc-(14)-MurNAc and peptide chains thatlink the glycans. PGN is recognized by the innate immune receptor
proteins, Nod1 and Nod2, in cytosol. We have established thesynthesis and then made the compound library of PGN fragments,
which would currently be the one of the most comprehensive libraryin the world. Based on the fragment library, we have analyzed thestructure-biology relationships of PGN in the recognition by Nod1
and Nod2, and also found natural Nod1 ligands in the environment.1
We have also recently revealed that Mycobacterium PGN fragments
exhibited very weak hNod1 and hNod2 activation, which provide a
potential mechanism for M. tuberculosis cytosolic immune evasion.2
Referecnes:
1.Fujimoto, Y.; Pradipta, A. R.; Inohara, N.; Fukase, K. Nat. Prod.
Rep. 2012, 29, 568.
2. Wang, Q.; Matsuo, Y.; Pradipta, A. R.; Inohara, N.: Fujimoto,Y.; Fukase, K. Org. Biomol. Chem., 2016, 14, 1013.

－5－

Nucleic Acid Sensing by Toll-like Receptors
Kensuke Miyake
Division of Innate Immunity, The Institute of Medical Science,
The University of Tokyo
kmiyake@ims.u-tokyo.ac.jp
The Toll family of receptors has critical roles in microbial
recognition and activation of defense responses. Nucleic acid (NA) isa major Toll-like receptor (TLR) ligand. TLR3, 7/8, and 9 reside in
intracellular organelle and sense double strand (ds) RNA, single
strand (ss) RNA, and ssDNA, respectively. A variety of vaccines
have been developed by modifying NAs. It is important tounderstand how NAs are sensed by TLRs. Recently reported TLR9
structure shows that TLR9 binds to short ssDNA fragment. dsDNA istherefore needed to be processed into short ssDNA fragments. DNase
II is the one and only DNase functioning in lysosomes. We recently
show that DNase II has an important role in processing CpG-A, anoligoDNA strongly inducing type I interferon production inplasmacytoid dendritic cells. CpG-A needs to be cleaved by DNase II
into a ssDNA fragment to stimulate TLR9. To develop novel DNA
vaccines, it is important to consider how DNAs are metabolized
before stimulating TLR9. Small chemical ligands for TLR7 andTLR8 are already used to stimulate immune responses in humans.
The structure of TLR8 reveals that a small chemical ligand binds todimerization interface of TLR8. Another structure of TLR8 with
ssRNA shows that TLR8 binds to uridine and di-ribonucleotide UG
instead of ssRNA fragment. TLR8 shows higher responses to Uridine
and ssRNA than ssRNA alone. TLR8 interaction with Uridine isenhanced in the presence of ssRNA. TLR8 is likely to sense Uridine
and oligoribonucleotides. Functional studies further show that TLR7
responds to Guanosine and ssRNA. These results indicate that TLR7
and TLR8 respond to a ribonucleoside with oligoribonucleotide.
Further study on the role of ribonucleosides in TLR7/8 responses
would contribute to development of novel vaccines.

－6－

Identification of a Novel Glycolipid Essential for
Membrane Protein Integration
Keiko Shimamoto
Suntory Foundation for Life Sciences, Bioorganic Research Instituteshimamot@sunbor.or.jp
Protein integration into membranes is a major biological event incells. The process of integration of membrane proteins into
biological membranes is basically conserved in all organisms. In
Escherichia coli, protein integration depends on a translocon that is
termed as the SecYEG/SRP (signal recognition particle) system(Figure 1A). In addition, the Sec/SRP-independent pathway is known
for a subset of membrane proteins. Recently, Nishiyama et al.
suggested the presence of an unknown factor, which is indispensable
in both Sec/SRP-dependent and -independent processes, and named
it MPIase (membrane protein integrase) after its function.1
We attempted to identify the factor and elucidate its mode of action.2
After many trial and error processes, repeated partition
chromatography yielded highly pure MPIase. When the purified
MPIase was added into liposomes, in which spontaneous integration
was inhibited, a substrate protein (3L-Pf3 coat) was
dose-dependently integrated into the liposomes. Moreover,stoichiometric analysis indicated that the number of integrated
substrate was higher than that of MPIase; i.e., MPIase catalyticallydrove 3L-Pf3 coat integration reactions.
Despite its enzyme-like activity, amino acid analysis indicated that
MPIase is non-proteinaceous and comprises unstable aminosugars.
GC–MS analysis after the methanolysis demonstrated the presence of
DAG containing typical of E. coli fatty acids. NMR studies of thepurified MPIase supported that it is a glycolipid. A pyrophosphate
linker between the reducing terminal of the glycan and lipid moiety
was demonstrated on 31P-NMR of MPIase.

－7－

The breakthrough for the structure determination of glycan was
MALDI-TOF-MS measurements. A characteristic series of peaks
suggested that MPIase contained repeating units. MS/MS analyses
indicated that the unit contained three components corresponding topartially O-acetylated N-acetyl-aminodeoxyhexose, N-acetyl-aminohexose, and N-acetyl-aminohexuronic acid. Removal of lipid andO-acetyl moieties by mild hydrolysis of MPIase gave a simpler MS
spectrum, suggesting that MPIase is a mixture of homologous
molecules with 9-11 repeating units in the glycan part.
Methanolysis of the glycan gave three major peaks on GC–MS, oneof which proved to be glucosamine (GlcNAc). We assumed thepresence of 4-acetamido-4-deoxyfucose (Fuc4NAc) from the
ROESY spectrum and synthesized authentic Fuc4NAc, which was
identical to another peak. Comparison of the remaining peak in
GC–MS spectrum with some synthesized authentic uronic acids
identified it as 2-acetamido- 2-deoxymannuronic acid (ManNAcA).
The sequence and linkage mode of the trisaccharide were determinedby 2D-NMR and confirmed by synthesis of trisaccharide unit.
Taking the aforementioned information into account, we determined
the structure of MPIase to be as shown in Figure 1B.
Direct interaction between the acetyl groups of glycan of MPIase and
3L-Pf3 coat protein was confirmed in saturation transfer differenceNMR. Although studies to elucidate the mechanisms of MPIase are
now in progress, we speculated that its glycan captures substrate
proteins to maintain an integration-competent structure (Figure 1C).
Although MPIase is a glycolipid devoid of a proteinaceous moiety,
MPIase exhibited integration-dedicated chaperone-like activity thatdrove subsequent membrane integration. On the basis of these results,
the term “glycolipozyme” was coined to express the enzyme-like
activity of MPIase.

－8－A. Membrne Protein Integration Pathways in E. coli
Translocon (SecYEG/SRP)‐dependent Pathway
Inner membrane

Ribozome

SR
M

SRP

Cytosol

Chaperone

Sec YEG

Signal Recognition

SRP: Signal Recognition Particle
SR: SRP receptor

MPIase (Membrane Protein Integrase)

Sec/SRP‐independent
PathwayM
3L‐Pf3 coatB. Structure of MPIaseO

C. Plausible Working Model

NH
O

O

O

Partial 6‐O‐Acetylation

OH HO2C HN
O
O
HO
O
HO

Fuc4NAc
ManNAcA

Integration

OR R = H or
O
O

NH
nO

GlcNAcPyrophosphate Linker
O

O

P O

P
O-

O-

Aggregation

O

CaptureOO

Trisaccharide Unit
( n = 9‐11)

SolubilizationO

O

MPIaseO

Diacylglycerol(Lipid Moiety)

Figure 1. A) Membrane protein pathway in E. coli. B) Structureof MPIase. C) Plausible working model of MPIase in 3L-Pf3
integration.

Referecnes:
1. K. Nishiyama, M. Maeda, M. Abe, T. Kanamori, K. Shimamoto, S.
Kusumoto, T. Ueda, and H. Tokuda, Biochem. Biophys. Res.
Commun., 394, 733 (2010).
2. K. Nishiyama, M. Maeda, K. Yanagisawa, R. Nagase, H. Komura,T. Iwashita, T. Yamagaki, S. Kusumoto, H. Tokuda, and K.
Shimamoto, Nat. Commun., 3, 1260 (2012).

－9－

Quest for Synthetic Chemistry’s Initiativein Glycobiology
Yukishige Ito
Synthetic Cellular Chemistry Laboratory, RIKEN and
ERATO Glycotrilogy Project, JSTyukito@riken.jp
The fields of “Glycobiology” and “Glycotechnology” are gaining an
increasing amount of attention. Glycoconjugates, such as
glycoproteins, glycolipids, proteoglycans, and microbial cell-surface
components, consist of glycan chains. A major part of our researchhas been directed at the synthesis and functional analysis ofglycoconjugate oligosaccharides of various origins.
Biological functions of glycoconjugate glycan chains are numerous.
Most typically, these molecules exist at the cell surface and play
numerous roles in cellular communication events, such as cell
migration, cell-matrix and cell-cell attachment, signal transduction,
microbial transfection, cancer metastasis, cell differentiation, andimmune responses. They also play fundamental roles in thestabilization of glycoproteins, modulating the 3-D structure and interand intracellular transport of proteins.
In order to gain a precise understanding of the functions of glycan
chains, access to structurally defined oligosaccharides is required.
Eukaryotic cells contain a huge number of glycoproteins.
Furthermore, structures of glycoprotein glycan chains are highly
diverse. In many cases, glycoproteins consist of various glycoforms,
which differ in the number, composition, branching, or terminal
modification of glycan chains. Therefore, the isolation of ahomogeneous glycoprotein with a defined structure is an extremely
difficult task, unless the target protein is exceptionally abundant.
Structures of glycoproteins are characterized by their complexity anddiversity. To clarify their functions, synthetic approaches are
considered to be promising. Development of synthetic methodologies－10－useful for efficient and facile preparation of oligosaccharides is a
focal issue in carbohydrate chemistry. In light of their structural
diversity, practical strategy to facilitate the synthesis ofoligosaccharide is expected to be highly valuable. Glycoprotein
glycans are known to play numerous biological roles, both intra- andintra-cellularly, through their interaction with various proteins suchas lectins, glycosidases, and glycosyltransferases. However, theirprecise analysis has been hindered by structural heterogeneity ofglycoproteins.
Given these circumstances, our effort has been directed to synthesisof glycoprotein glycans and related probes for analysis of theirintracellular functions. This talk will cover selected topics among ourrecent studies on 1) development of novel methods for selective
formation of glycosidic linkages,1-3 2) target-oriented as well as
library oriented synthesis of glycoprotein glycans,4 3) analysis ofglycan-protein interactions in the ER using synthetic substrates,5-11
and 4) mechanistic studies on carbohydrate binding agents.12

Referecnes:
1.
2.
3.
4.
5.
6.
7.
8.
9.
10.
11.
12.

A. Ishiwata, et al., JACS, 133, 19524 (2011); JACS, 133, 2275 (2011)
A. Ishiwata, et al., OBC, 8, 3596 (2010); ACIE, 53, 9812 (2014)
H. Satoh, et al., JACS, 133, 5610 (2011); S. Manabe et al., CEJ, 20, 124(2014)
A. Koizumi, et al., ACIE, 52 7426 (2013); K. Fujikawa et al., CEJ, 21,3224 (2015)
Y. Ito, et al., Sem. Dev. Cell. Biol., 41, 90 (2015)
K. Totani, et al., Biochemistry, 48, 2933 (2009)
Y. Takeda et al., Glycobiology, 24, 344 (2014)
K. Ohara et al., Biochemistry, 54, 4909 (2015)
M. Sakono, et al., BBRC, 426, 504 (2012)
M. Hachisu et al., ChemBioChem, doi.org/10.1002/cbic.201500595
M. Izumi et al., JACS, 134, 7238 (2012)
Y. Nakagawa, et al., ACIE, 50 6084 (2011); JACS, 133, 17485 (2011);
CEJ, 19, 10516 (2013)－11－

Chemistry and Biological Functions of Bacterial
Cell Surface Glycoconjugates
Shoichi Kusumoto
Professor Emeritus, Osaka University
skus@w8.dion.ne.jp

Since the middle of the 20th century, certain bacterial cellcomponents were known to nonspecifically enhance theimmunological responses of higher animals. These were earlyobservations of a new defense system of animals, which is now wellknown as innate immunity. Our research group fortunately foundopportunities to join this research area and succeeded in
identification of the active chemical entities of the immune
stimulatory functions of both bacterial cell wall peptidoglycan (PGN)
and bacterial endotoxin.
In 1942 Freund et al. first described that heat-killed Mycobacterium
cells enhanced production of antibody against given protein antigens.
Several research groups then proved that PGN ubiquitously
distributed on both gram-positive and -negative bacterial cells is
responsible for this function. Kotani and his group found thatoligosaccharide peptide fractions obtained by controlled enzymatic
digestion of PGN showed definite activity to enhance theimmunological responses of experimental animals in a way similar tothat by intact bacterial cells. In order to identify the active entity,
several synthetic N-acetylmuramyl peptides from our laboratory
weretestedbyKotani’sgroup.
Amongthem,
N-acetylmuramyl-L-alanyl-D-isoglutamine (abbreviated muramyl
dipeptide, MDP) was found to exhibit definite activity and thus
proved to be the smallest active structure of PGN. It was a quite
impressive fact at that time that a small molecular species like MDP
represents the function of the entire complex bacterial highmolecular component PGN.

－12－

During the above study on PGN, we came to know another, morepotent bacterial cell surface constituent, “endotoxin”, which was firstdescribed by Pfeiffer in 1892 as a potent toxic component of Vibrio
cholera cells. Westphal and Lüderitz then disclosed that chemical
entity of endotoxin is lipopolysaccharide (LPS) which is a common
constituent of all gram-negative bacteria. They also described in
1954 that the lipophilic part of LPS, which they named “lipid A”, isthe endotoxic active principle.
In spite of intensive investigations by Lüderitz and his successors,
the complete and precise chemical structure of lipid A was not
elucidated until we succeeded in isolation of a single homogeneous
molecular species of a lipid A derivative in 1984. Our chemical andspectroscopic analyses of the purified derivative led to the precise
structure of lipid A as an N,O-polyacylated glucosiamine
disaccharide bisphosphate. This conclusion was immediately
confirmed by our total chemical synthesis of the proposed structure
in 1984: the synthetic lipid A exhibited identical, full biologicalactivities with those of bacterial endotoxin. This was the final
unequivocal proof of the concept that lipid A is the active entity ofbacterial endotoxin after hundred years of time since its discovery.
After that, precise studies had become possible of the action
mechanism of lipid A by the use of synthetic homogeneous
preparation and various structural analogues. It was also shown that
excessive activation of immune competent cells resulted in serious
damage of animals such as high fever, tissue and organ damages,
organ failure, or even death of host animals, which was recognized as
toxic effects of endotoxin. Around the end of the 20th century, agroup of specific receptors named Toll-like receptors (TLRs) was
discovered on animal cell membrane. Among them TLR4 wasproved to be the specific receptor for endotoxin. The Nobel Prize inPhysiology or Medicine in 2011 went to Bruce A. Beutler for his
contribution with this regard.
The elaborate defense system of higher animals against invading
pathogens was hence disclosed around this period: animals are well
prepared by born by having, for example TLR4 which specifically－13－

recognizes endotoxin/lipid A as a signal of invading gram-negative
microbes and switches further immunological defense system on toprevent further invasion. In the meantime, another protein Nod2 was
discovered and was proved to be a specific receptor for MDP. Thismeans MDP, as another common bacterial cell constituent, also acts
as a trigger of the innate immune system.
Thinking back the time when we started our research in this line,
nothing was known at all on the innate immune system. We were justsimply but strongly interested in the fact that certain bacteria cellsurface components, which are normally never present in our own
body, activate our defense system: we anticipated the presence of any
unknown general defense mechanism. We were thus quite lucky inthe point that we came into this expanding but old research field of
immunology just on a right moment and were able to contribute to
the new development of the research from a side of organic chemists.
We very much appreciate the many researchers worldwide for theirenjoyable and fruitful interdisciplinary collaborations for over three
decades. Now that the research reached to a stage where molecularbiological techniques show their strong power, I myself feel that therole of organic chemists in this field became unfortunately lessimportant than before.
References:
1.

2.
3.

Key
structuresofbacterial
peptidoglycan
andlipopolysaccharide triggering the innate immune system ofhigher animals: Chemical synthesis and functional studies. S.
Kusumoto, K. Fukase, T. Shiba, Proc. Japan Acad. Ser. B 2010,
86 (4), 322-337.
Synthesis of endotoxic principle of bacterial lipopolysaccharide
and its recognition by the innate immune systems of hosts. S.
Kusumoto, K. Fukase, Chem. Rec., 2006, 6, 333-343.
Synthetic and natural Escherichia coli free lipid A express
identical endotoxic activities.C. Galanos, O. Lüderitz, E. Th.
Rietschel, O. Westphal, H. Brade, L. Brade, M. Freudenberg, U.
Schade, M. Imoto, H. Yoshimura, S. Kusumoto, and T. Shiba,
Eur. J. Biochem., 1985, 148, 1-5.

－14－

Yukari Fujimoto: born in 1967 andgraduated (B. 1989), and received Ph. D.
(2002) from Osaka University (Prof.
Shoichi Kusumoto). After industrial
experience at Sumitomo Chemical Co., Ltd.,
post-graduate
studiesatColumbia
University(1998-2001,
Prof.
Koji
Nakanishi), and postdoctoral studies at
Nagoya University (2002, Prof. Yoshihito
Watanabe), she joined the faculty of Osaka
University, as Assistant Professor (2003-2006) (Profs. Shoichi
Kusumoto, and Koichi Fukase), then Lecturer (2006-2008), andAssociate Professor (2008-2014). Moverd to Keio University as a
Proefessor (2014-). Several awards including Incentive Award in
Synthetic Organic Chemistry from the Society for Synthetic Organic
Chemistry and the Alois Nowotny Award from International
Endotoxin & Innate Immunity Society.

Kensuke Miyake is a professor of theDivision of Innate Immunity, Departmentof Microbiology and Immunology, The
Institute of Medical Science, The
University of Tokyo. He graduated from
Okayama University Medical School in
1984, and obtained Ph.D. at Osaka
University Medical School in 1988. He
joined the laboratory of Dr. Paul W.
Kincade as a postdoctoral fellow in
Oklahoma Medical Research foundation from 1988-1990. He thenreturned to Japan and joined the laboratory of Dr. Masao Kimoto in
the Department of Immunology, Saga Medical School in1990. He
moved to the University of Tokyo in 2001, and has been in thecurrent position.

－15－

Keiko Shimamoto born in Kobe, 1962 andgraduated from 1984 Osaka University,
1991, Osaka University, Prof. Shoichi
Kusumoto.
Keiko
Shimamotostudiedorganicsynthesis at Osaka University under the
direction of Prof. Tetsuo Shiba andreceived her M.S. degree in 1986. She
joined Suntory Institute for Bioorganic
Research (SUNBOR) in 1986 and is
working there as an executive researcher. She received her Ph.D.
from Osaka University in 1991 under the supervision of Prof.
Shoichi Kusumoto. Her research interests include the investigation of
the functions of bioactive amino acids and glycolipids based on thesynthesis of novel molecular probes. She was awarded the
Yamazaki–Teiichi Prize in 2006 and the Chemical Society of Japan
Award for Creative Work for 2013.
Yukishige Ito: born in 1954 and graduatedfrom The University of Tokyo (B. 1977)
PhD, The University of Tokyo (Prof. Masaji
Ohno)
1982,
Postdoctoral
fellow,
Massachusetts Institute of Technology(1982-1984, Prof. Satoru Masamune),
Research Scientist (1984-1996), RIKEN,
Senior Scientist (1996-1998), Chief
Scientist (1998-), Synthetic Cellular
Chemistry Laboratory, RIKEN, Visiting
Scholar, Cytel Corporation and the Scripps Research Institute(1991-1993), Research Director, JST ERATO Glycotrilogy Project(2009-2015). Received awards include Whistler International Award
in Carbohydrate Chemistry, Japan Society for Bioscience,
Biotechnology, and Agrochemistry Award.

－16－

The Recipients of the Prize hereto are:1996 Yoshimasa Hirata*
2007 Hung-wen Liu
1997 Frank H. Westheimer
2008 Michel Rohmer*
1998 Albert J. Eschenmoser*
2009 JoAnne Stubbe
1999 Jeremy R. Knowles
2010 Shosuke Yamamura*2000 Satoshi Ōmura*2011 C. Dale Poulter2001 John D. Roberts
2012 Daisuke Uemura*
2002 Sir Jack Baldwin*
2013 Arthur G. Palmer, III
2003 A. Ian Scott2014 Jerrold Meinwald*
2004 Isao Kitagawa*2015 Fred McLafferty
2005 Stephen J. Benkovic
2016 Shoichi Kusumoto*2006 Takeshi Yasumoto**Selection and presentation made by the Chemical Society of Japan.

Organizing Committee:◆Chairman
Minoru Ueda (Tohoku University)◇Members
Ikuro Abe (The University of Tokyo)
Yukari Fujimoto (Keio University)
Michio Murata (Osaka University)
Hiroyuki Osada (RIKEN)
Naoki Sugimoto (Konan University)

Keisuke Suzuki (Tokyo Institute of Technology)
Daisuke Uemura (Kanagawa University)－17－