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Article ; Online: Function of the glycosyltransferase GnT-V in colitis.

Nonaka, Motohiro

2016 Volume 51, Issue 4, Page(s) 406–408

MeSH term(s)	Colitis ; Glycosyltransferases ; Humans ; N-Acetylglucosaminyltransferases
Chemical Substances	Glycosyltransferases (EC 2.4.-) ; N-Acetylglucosaminyltransferases (EC 2.4.1.-)
Language	English
Publishing date	2016-04
Publishing country	Japan
Document type	Comment ; Editorial
ZDB-ID	1186495-3
ISSN	1435-5922 ; 0944-1174
ISSN (online)	1435-5922
ISSN	0944-1174
DOI	10.1007/s00535-015-1156-y
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Article: Design and Synthesis of Monobody Variants with Low Immunogenicity.

Iwamoto, Naoya / Sato, Yukino / Manabe, Asako / Inuki, Shinsuke / Ohno, Hiroaki / Nonaka, Motohiro / Oishi, Shinya

ACS medicinal chemistry letters

2023 Volume 14, Issue 11, Page(s) 1596–1601

Abstract: Mirror-image proteins (d-proteins) are promising scaffolds for drug discovery because of their high proteolytic stability and low immunogenic properties. Facile and reproducible processes for the preparation of functional d-proteins are required for ... ...

Abstract	Mirror-image proteins (d-proteins) are promising scaffolds for drug discovery because of their high proteolytic stability and low immunogenic properties. Facile and reproducible processes for the preparation of functional d-proteins are required for their application in therapeutic biologics. In this study, we designed and synthesized a novel monobody variant with two cysteine substitutions that facilitate the synthetic process via sequential native chemical ligations and improve protein stability by disulfide bond formation. The synthetic anti-GFP monobody in this model study exhibited good binding affinity to the target enhanced green fluorescent protein. In vivo administration of the synthetic anti-GFP monobody (l-monobody) to mice induced antidrug antibody (ADA) production, whereas no ADA production was observed following immunization with the mirror-image anti-GFP monobody (d-monobody). These results suggest that the synthetic d-monobody is a non-antibody protein scaffold with low immunogenic properties.
Language	English
Publishing date	2023-10-09
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.3c00342
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Article ; Online: Screening of a library of traditional Chinese medicines to identify compounds and extracts which inhibit Toxoplasma gondii growth.

Saito, Harunobu / Murata, Yuho / Nonaka, Motohiro / Kato, Kentaro

The Journal of veterinary medical science

2020 Volume 82, Issue 2, Page(s) 184–187

Abstract: Toxoplasma gondii can cause severe encephalitis in immunocompromised patients. Although pyrimethamine and sulphadiazine have been standard therapeutic agents for the treatment of acute toxoplasmosis, they have toxic side effects. Therefore, there is a ... ...

Abstract	Toxoplasma gondii can cause severe encephalitis in immunocompromised patients. Although pyrimethamine and sulphadiazine have been standard therapeutic agents for the treatment of acute toxoplasmosis, they have toxic side effects. Therefore, there is a need to identify new drugs that are less toxic. Some traditional Chinese medicines (TCMs) have shown good efficacy in controlling T. gondii replication in mouse models. Here, we screened a natural product library comprising TCMs with the aim of identifying compounds and extracts with anti-toxoplasmosis activities. We found several hit compounds and extracts that could be candidates for new drugs against T. gondii infection.
MeSH term(s)	Animals ; Antiprotozoal Agents/adverse effects ; Antiprotozoal Agents/pharmacology ; Cell Line ; Chlorocebus aethiops ; Drugs, Chinese Herbal/adverse effects ; Drugs, Chinese Herbal/pharmacology ; Humans ; Toxoplasma/drug effects ; Toxoplasma/growth & development ; Toxoplasmosis/drug therapy ; Vero Cells
Chemical Substances	Antiprotozoal Agents ; Drugs, Chinese Herbal
Language	English
Publishing date	2020-01-02
Publishing country	Japan
Document type	Journal Article
ZDB-ID	1071753-5
ISSN	1347-7439 ; 0916-7250
ISSN (online)	1347-7439
ISSN	0916-7250
DOI	10.1292/jvms.19-0241
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Article ; Online: Construction of a T7 phage random peptide library by combining seamless cloning with in vitro translation.

Higashi, Katsuaki / Oda, Sakiho / Fujii, Mai / Nishida, Fumiya / Matsumoto, Hayato / Morise, Jyoji / Oka, Shogo / Nonaka, Motohiro

Journal of biochemistry

2023 Volume 175, Issue 1, Page(s) 85–93

Abstract: T7 phage libraries displaying random peptides are powerful tools for screening peptide sequences that bind to various target molecules. The T7 phage system has the advantage of less biased peptide distribution compared to the M13 phage system. However, ... ...

Abstract	T7 phage libraries displaying random peptides are powerful tools for screening peptide sequences that bind to various target molecules. The T7 phage system has the advantage of less biased peptide distribution compared to the M13 phage system. However, the construction of T7 phage DNA is challenging due to its long 36 kb linear DNA. Furthermore, the diversity of the libraries depends strongly on the efficiency of commercially available packaging extracts. To address these issues, we examined the combination of seamless cloning with cell-free translation systems. Seamless cloning technologies have been widely used to construct short circular plasmid DNA, and several recent studies showed that cell-free translation can achieve more diverse phage packaging. In this study, we combined these techniques to construct four libraries (CX7C, CX9C, CX11C and CX13C) with different random regions lengths. The libraries thus obtained all showed diversity > 109 plaque forming units (pfu). Evaluating our libraries with an anti-FLAG monoclonal antibody yielded the correct epitope sequence. The results indicate that our libraries are useful for screening peptide epitopes against antibodies. These findings suggest that our system can efficiently construct T7 phage libraries with greater diversity than previous systems.
MeSH term(s)	Peptide Library ; Amino Acid Sequence ; Bacteriophage T7/genetics ; Bacteriophage T7/metabolism ; Peptides/chemistry ; DNA/metabolism ; Epitopes/chemistry ; Cloning, Molecular
Chemical Substances	Peptide Library ; Peptides ; DNA (9007-49-2) ; Epitopes
Language	English
Publishing date	2023-10-05
Publishing country	England
Document type	Journal Article
ZDB-ID	218073-x
ISSN	1756-2651 ; 0021-924X
ISSN (online)	1756-2651
ISSN	0021-924X
DOI	10.1093/jb/mvad077
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Article ; Online: Mirror-Image Single-Domain Antibody for a Novel Nonimmunogenic Drug Scaffold.

Aoki, Keisuke / Manabe, Asako / Kimura, Hiroyuki / Katoh, Yohei / Inuki, Shinsuke / Ohno, Hiroaki / Nonaka, Motohiro / Oishi, Shinya

Bioconjugate chemistry

2023 Volume 34, Issue 11, Page(s) 2055–2065

Abstract: Immunogenic responses by protein therapeutics often lead to reduced therapeutic effects and/or adverse effects via the generation of neutralizing antibodies and/or antidrug antibodies (ADA). Mirror-image proteins of the variable domain of the heavy chain ...

Abstract	Immunogenic responses by protein therapeutics often lead to reduced therapeutic effects and/or adverse effects via the generation of neutralizing antibodies and/or antidrug antibodies (ADA). Mirror-image proteins of the variable domain of the heavy chain of the heavy chain antibody (VHH) are potential novel protein therapeutics with high-affinity binding to target proteins and reduced immunogenicity because these mirror-image VHHs (d-VHHs) are less susceptible to proteolytic degradation in antigen-presenting cells (APCs). In this study, we investigated the preparation protocols of d-VHHs and their biological properties, including stereoselective target binding and immunogenicity. Initially, we established a facile synthetic process of two model VHHs [anti-GFP VHH and PMP12A2h1 (monomeric VHH of caplacizumab)] and their mirror-image proteins by three-step native chemical ligations (NCLs) from four peptide segments. The folded synthetic VHHs (l-anti-GFP VHH and l-PMP12A2h1) bound to the target proteins (EGFP and vWF-A1 domain, respectively), while their mirror-image proteins (d-anti-GFP VHH and d-PMP12A2h1) showed no binding to the native proteins. For biodistribution studies, l-VHH and d-VHH with single radioactive indium diethylenetriamine-pentaacid (
MeSH term(s)	Mice ; Animals ; Single-Domain Antibodies ; Pharmaceutical Preparations ; Tissue Distribution ; Immunoglobulin Heavy Chains ; Antibodies, Neutralizing ; Camelids, New World/metabolism
Chemical Substances	Single-Domain Antibodies ; Pharmaceutical Preparations ; Immunoglobulin Heavy Chains ; Antibodies, Neutralizing
Language	English
Publishing date	2023-10-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1024041-x
ISSN	1520-4812 ; 1043-1802
ISSN (online)	1520-4812
ISSN	1043-1802
DOI	10.1021/acs.bioconjchem.3c00372
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Article ; Online: Engineering a Low-Immunogenic Mirror-Image VHH against Vascular Endothelial Growth Factor.

Aoki, Keisuke / Higashi, Katsuaki / Oda, Sakiho / Manabe, Asako / Maeda, Kayuu / Morise, Jyoji / Oka, Shogo / Inuki, Shinsuke / Ohno, Hiroaki / Oishi, Shinya / Nonaka, Motohiro

ACS chemical biology

2024

Abstract: Immunogenicity is a major caveat of protein therapeutics. In particular, the long-term administration of protein therapeutic agents leads to the generation of antidrug antibodies (ADAs), which reduce drug efficacy while eliciting adverse events. One ... ...

Abstract	Immunogenicity is a major caveat of protein therapeutics. In particular, the long-term administration of protein therapeutic agents leads to the generation of antidrug antibodies (ADAs), which reduce drug efficacy while eliciting adverse events. One promising solution to this issue is the use of mirror-image proteins consisting of d-amino acids, which are resistant to proteolytic degradation in immune cells. We have recently reported the chemical synthesis of the enantiomeric form of the variable domain of the antibody heavy chain (d-VHH). However, identifying mirror-image antibodies capable of binding to natural ligands remains challenging. In this study, we developed a novel screening platform to identify a d-VHH specific for vascular endothelial growth factor A (VEGF-A). We performed mirror-image screening of two newly constructed synthetic VHH libraries displayed on T7 phage and identified VHH sequences that effectively bound to the mirror-image VEGF-A target (d-VEGF-A). We subsequently synthesized a d-VHH candidate that preferentially bound the native VEGF-A (l-VEGF-A) with submicromolar affinity. Furthermore, immunization studies in mice demonstrated that this d-VHH elicited no ADAs, unlike its corresponding l-VHH. Our findings highlight the utility of this novel d-VHH screening platform in the development of protein therapeutics exhibiting both reduced immunogenicity and improved efficacy.
Language	English
Publishing date	2024-05-02
Publishing country	United States
Document type	Journal Article
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.4c00197
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Article ; Online: THE EFFICACY OF MARINE NATURAL PRODUCTS AGAINST PLASMODIUM FALCIPARUM.

Goto, Yukihiro / Kamihira, Rie / Nakao, Yoichi / Nonaka, Motohiro / Takano, Ryo / Xuan, Xuenan / Kato, Kentaro

The Journal of parasitology

2021 Volume 107, Issue 2, Page(s) 284–288

Abstract: Malaria remains one of the most important infectious diseases in the world. In 2017 alone, approximately 219 million people were infected with malaria, and 435,000 people died of this disease. Plasmodium falciparum, which causes falciparum malaria, is ... ...

Abstract	Malaria remains one of the most important infectious diseases in the world. In 2017 alone, approximately 219 million people were infected with malaria, and 435,000 people died of this disease. Plasmodium falciparum, which causes falciparum malaria, is becoming resistant to artemisinin (ART) in Southeast Asia; therefore, new antimalarial drugs are urgently needed. Some excellent antimalarial drugs, such as quinine and ART, were originally obtained from plants. Hence, we analyzed the antimalarial effects of marine natural products to find new antimalarial agents. We used a malaria growth inhibition assay to determine the antimalarial ability and half-maximal inhibitory concentration (IC50) values of the marine organism-derived compounds. Three compounds (kapakahine A, kapakahine B, and kulolide-1) showed antimalarial effects, and one (kapakahine F) showed selective antimalarial effects on the Dd2 clone. Although the IC50 values obtained for these compounds were greater than that of ART, their potency against P. falciparum is sufficient to warrant further investigation of these compounds as possible drug leads.
MeSH term(s)	Antimalarials/chemistry ; Antimalarials/pharmacology ; Antimalarials/therapeutic use ; Humans ; Inhibitory Concentration 50 ; Malaria, Falciparum/drug therapy ; Marine Toxins/chemistry ; Marine Toxins/pharmacology ; Peptides, Cyclic/chemistry ; Peptides, Cyclic/pharmacology ; Peptides, Cyclic/therapeutic use ; Plasmodium falciparum/drug effects
Chemical Substances	Antimalarials ; Marine Toxins ; Peptides, Cyclic ; kapakahine A ; kapakahine B ; kulolide-1
Language	English
Publishing date	2021-04-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	300870-8
ISSN	1937-2345 ; 0022-3395
ISSN (online)	1937-2345
ISSN	0022-3395
DOI	10.1645/20-93
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Article ; Online: Distinct Cell Surface Expression Patterns of N-Glycosylation Site Mutants of AMPA-Type Glutamate Receptor under the Homo-Oligomeric Expression Conditions.

Morise, Jyoji / Yamamoto, Saki / Midorikawa, Ryosuke / Takamiya, Kogo / Nonaka, Motohiro / Takematsu, Hiromu / Oka, Shogo

International journal of molecular sciences

2020 Volume 21, Issue 14

Abstract: The AMPA-type glutamate receptor (AMPAR) is a homotetrameric or heterotetrameric ion channel composed of various combinations of four subunits (GluA1-4), and its abundance in the synapse determines the strength of synaptic activity. The formation of ... ...

Abstract	The AMPA-type glutamate receptor (AMPAR) is a homotetrameric or heterotetrameric ion channel composed of various combinations of four subunits (GluA1-4), and its abundance in the synapse determines the strength of synaptic activity. The formation of oligomers in the endoplasmatic reticulum (ER) is crucial for AMPAR subunits' ER-exit and translocation to the cell membrane. Although N-glycosylation on different AMPAR subunits has been shown to regulate the ER-exit of hetero-oligomers, its role in the ER-exit of homo-oligomers remains unclear. In this study, we investigated the role of N-glycans at GluA1N63/N363 and GluA2N370 in ER-exit under the homo-oligomeric expression conditions, whose mutants are known to show low cell surface expressions. In contrast to the N-glycosylation site mutant GluA1N63Q, the cell surface expression levels of GluA1N363Q and GluA2N370Q increased in a time-dependent manner. Unlike wild-type (WT) GluA1, GluA2WT rescued surface GluA2N370Q expression. Additionally, the expression of GluA1N63Q reduced the cell surface expression level of GluA1WT. In conclusion, our findings suggest that these N-glycans have distinct roles in the ER-exit of GluA1 and GluA2 homo-oligomers; N-glycan at GluA1N63 is a prerequisite for GluA1 ER-exit, whereas N-glycans at GluA1N363 and GluA2N370 control the ER-exit rate.
MeSH term(s)	Amino Acid Substitution ; Binding Sites/genetics ; Cell Membrane/metabolism ; Gene Expression ; Glycosylation ; Green Fluorescent Proteins/chemistry ; Green Fluorescent Proteins/genetics ; Green Fluorescent Proteins/metabolism ; HEK293 Cells ; Humans ; Mutagenesis, Site-Directed ; Mutation ; Protein Structure, Quaternary ; Receptors, Glutamate/chemistry ; Receptors, Glutamate/genetics ; Receptors, Glutamate/metabolism ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism
Chemical Substances	Receptors, Glutamate ; Recombinant Fusion Proteins ; alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid subtype glutamate receptor, human ; Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2020-07-19
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms21145101
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Article ; Online: Functional assay using lectin gene targeting technologies (over-expression).

Nonaka, Motohiro / Kawasaki, Toshisuke

Methods in molecular biology (Clifton, N.J.)

2014 Volume 1200, Page(s) 389–399

Abstract: Function of lectin depends on its amino acid sequence of carbohydrate-recognition domain (CRD), conformation, and extracellular/intracellular localization. Altering lectin gene expression by over-expression or knockdown is a powerful tool for analyzing ... ...

Abstract	Function of lectin depends on its amino acid sequence of carbohydrate-recognition domain (CRD), conformation, and extracellular/intracellular localization. Altering lectin gene expression by over-expression or knockdown is a powerful tool for analyzing its cellular function. Here, we describe a method of lectin gene over-expression, taking a C-type lectin, mannan-binding protein (MBP), as an example. Carbohydrate-binding ability of MBP, its subcellular localization, and functional co-localization with ligand glycoprotein are assayed comparing with an inactive mutant MBP.
MeSH term(s)	Cell Line, Tumor ; Gene Expression ; Gene Targeting/methods ; HIV Envelope Protein gp120/genetics ; HIV Envelope Protein gp120/metabolism ; Humans ; Intracellular Space/metabolism ; Lectins/genetics ; Lectins/metabolism ; Lectins, C-Type/genetics ; Lectins, C-Type/metabolism ; Mannans/metabolism ; Mannose-Binding Lectin/genetics ; Mannose-Binding Lectin/metabolism ; Microspheres ; Mutation ; Plasmids/genetics ; Protein Transport ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism ; Transfection
Chemical Substances	HIV Envelope Protein gp120 ; Lectins ; Lectins, C-Type ; Mannans ; Mannose-Binding Lectin ; Recombinant Proteins
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-1292-6_34
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Article ; Online: Galectin-1 for neuroprotection?

Nonaka, Motohiro / Fukuda, Minoru

Immunity

2012 Volume 37, Issue 2, Page(s) 187–189

Abstract: Classically activated microglia (M1) are believed to play a key role in neuronal degeneration in multiple sclerosis (MS). In this issue of Immunity, Starossom et al. (2012) show that Galectin-1 exerts a neuroprotective function through glycosylation- ... ...

Abstract	Classically activated microglia (M1) are believed to play a key role in neuronal degeneration in multiple sclerosis (MS). In this issue of Immunity, Starossom et al. (2012) show that Galectin-1 exerts a neuroprotective function through glycosylation-dependent inactivation with M1 cells.
Language	English
Publishing date	2012-08-24
Publishing country	United States
Document type	Comment ; Journal Article
ZDB-ID	1217235-2
ISSN	1097-4180 ; 1074-7613
ISSN (online)	1097-4180
ISSN	1074-7613
DOI	10.1016/j.immuni.2012.08.006
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