2024/10/22 更新

写真a

カジ ヒロユキ
梶 裕之
KAJI Hiroyuki
所属
糖鎖生命コア研究所 糖鎖ビッグデータセンター 数理解析部門 特任教授
職名
特任教授
外部リンク

学位 1

  1. 理学博士 ( 1989年3月   青山学院大学 ) 

研究キーワード 5

  1. プロテオミクス

  2. グライコプロテオミクス

  3. 質量分析

  4. 翻訳後修飾

  5. 糖鎖修飾

経歴 2

  1. 名古屋大学   糖鎖生命コア研究所 糖鎖ビッグデータセンター 数理解析部門   特任教授

    2022年8月 - 現在

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  2. 名古屋大学   糖鎖生命コア研究所 統合生命医科学糖鎖研究センター数理解析部門   特任教授

    2022年4月 - 2022年7月

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所属学協会 3

  1. 日本糖質学会

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  2. 日本生化学会

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  3. 日本プロテオーム学会

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論文 16

  1. GRable Version 1.0: A Software Tool for Site-Specific fi c Glycoform Analysis With Improved MS1-Based Glycopeptide Detection With Parallel Clustering and Confidence fi dence Evaluation With MS2 Information 国際誌

    Nagai-Okatani, C; Tominaga, D; Tomioka, A; Sakaue, H; Goda, N; Ko, SGR; Kuno, A; Kaji, H

    MOLECULAR & CELLULAR PROTEOMICS   23 巻 ( 9 ) 頁: 100833 - 100833   2024年9月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Molecular and Cellular Proteomics  

    High-throughput intact glycopeptide analysis is crucial for elucidating the physiological and pathological status of the glycans attached to each glycoprotein. Mass spectrometry–based glycoproteomic methods are challenging because of the diversity and heterogeneity of glycan structures. Therefore, we developed an MS1-based site-specific glycoform analysis method named "Glycan heterogeneity-based Relational IDentification of Glycopeptide signals on Elution profile (Glyco-RIDGE)" for a more comprehensive analysis. This method detects glycopeptide signals as a cluster based on the mass and chromatographic properties of glycopeptides and then searches for each combination of core peptides and glycan compositions by matching their mass and retention time differences. Here, we developed a novel browser-based software named GRable for semi-automated Glyco-RIDGE analysis with significant improvements in glycopeptide detection algorithms, including "parallel clustering." This unique function improved the comprehensiveness of glycopeptide detection and allowed the analysis to focus on specific glycan structures, such as pauci-mannose. The other notable improvement is evaluating the "confidence level" of the GRable results, especially using MS2 information. This function facilitated reduced misassignment of the core peptide and glycan composition and improved the interpretation of the results. Additional improved points of the algorithms are "correction function" for accurate monoisotopic peak picking; one-to-one correspondence of clusters and core peptides even for multiply sialylated glycopeptides; and "inter-cluster analysis" function for understanding the reason for detected but unmatched clusters. The significance of these improvements was demonstrated using purified and crude glycoprotein samples, showing that GRable allowed site-specific glycoform analysis of intact sialylated glycoproteins on a large-scale and in-depth. Therefore, this software will help us analyze the status and changes in glycans to obtain biological and clinical insights into protein glycosylation by complementing the comprehensiveness of MS2-based glycoproteomics. GRable can be freely run online using a web browser via the GlyCosmos Portal (https://glycosmos.org/ grable).

    DOI: 10.1016/j.mcpro.2024.100833

    Web of Science

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  2. The Human Glycome Atlas Project for cataloging all glycan-related omics data in human.

    Aoki-Kinoshita KF, Ando H, Angata K, Fujita M, Furukawa JI, Kaji H, Kato K, Kitajima K, Kizuka Y, Matsui Y, Nakajima K, Nishihara S, Okajima T, Sakamoto K, Sato C, Thaysen-Andersen M, Togayachi A, Yagi H, Kadomatsu K

    Glycobiology     2024年7月

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    記述言語:英語  

    DOI: 10.1093/glycob/cwae052

    PubMed

  3. Glycosylation of recombinant adeno-associated virus 6 国際誌

    Yamaguchi, Y; Ishii, K; Koizumi, S; Sakaue, H; Maruno, T; Fukuhara, M; Shibuya, R; Tsunaka, Y; Matsushita, A; Bandoh, K; Torisu, T; Murata-Kishimoto, C; Tomioka, A; Mizukado, S; Kaji, H; Kashiwakura, Y; Ohmori, T; Kuno, A; Uchiyama, S

    MOLECULAR THERAPY METHODS & CLINICAL DEVELOPMENT   32 巻 ( 2 ) 頁: 101256 - 101256   2024年6月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)   出版者・発行元:Molecular Therapy Methods and Clinical Development  

    Glycosylation of biopharmaceuticals can affect their safety and efficacy. Glycans can occur on recombinant adeno-associated viruses (rAAVs) that are used for gene therapy; however, the types of glycans that attach to rAAVs are controversial. Here, we conducted lectin microarray analyses on six rAAV serotype 6 (rAAV6) preparations that were produced differently. We demonstrate that O-glycans considered to be attached to rAAV6 were recognized by Agaricus bisporus agglutinin (ABA) and that N-glycans were detected in rAAV6 purified without affinity chromatography. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis showed that the N-glycans detected in rAAV6 were derived from host cell proteins. A combination of ABA-based fractionation and LC-MS/MS revealed that rAAV6 was O-glycosylated with the mucin-type glycans, O-GalNAc (Tn antigen), and mono- and di-sialylated Galβ1-3GalNAc (T antigen) at S156, T162, T194, and T201 in viral protein (VP) 2 and with O-GlcNAc at T242 in VP3. The mucin-type O-glycosylated rAAV6 particles were 0.1%–1% of total particles. Further physicochemical and biological analyses revealed that mucin-type O-glycosylated rAAV6 had a lower ratio of VP1 to VP2/VP3, resulting in a lower transduction efficiency both in vitro and in vivo compared with rAAV6 without mucin-type O-glycans. This report details conclusive evidence of rAAV glycosylation and its impact on rAAV-based therapeutics.

    DOI: 10.1016/j.omtm.2024.101256

    Web of Science

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  4. Combinatorial Approach with Mass Spectrometry and Lectin Microarray Dissected Site-Specific Glycostem and Glycoleaf Features of the Virion-Derived Spike Protein of Ancestral and γ Variant SARS-CoV-2 Strains. 国際誌

    Takahiro Hiono, Hiroaki Sakaue, Azusa Tomioka, Hiroyuki Kaji, Michihito Sasaki, Yasuko Orba, Hirofumi Sawa, Atsushi Kuno

    Journal of proteome research   23 巻 ( 4 ) 頁: 1408 - 1419   2024年4月

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    記述言語:英語   掲載種別:研究論文(学術雑誌)  

    The coronavirus disease (COVID-19) pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has impacted public health globally. As the glycosylation of viral envelope glycoproteins is strongly associated with their immunogenicity, intensive studies have been conducted on the glycans of the glycoprotein of SARS-CoV-2, the spike (S) protein. Here, we conducted intensive glycoproteomic analyses of the SARS-CoV-2 S protein of ancestral and γ-variant strains using a combinatorial approach with two different technologies: mass spectrometry (MS) and lectin microarrays (LMA). Our unique MS1-based glycoproteomic technique, Glyco-RIDGE, in addition to MS2-based Byonic search, identified 1448 (ancestral strain) and 1785 (γ-variant strain) site-specific glycan compositions, respectively. Asparagine at amino acid position 20 (N20) is mainly glycosylated within two successive potential glycosylation sites, N17 and N20, of the γ-variant S protein; however, we found low-frequency glycosylation at N17. Our novel approaches, glycostem mapping and glycoleaf scoring, also illustrate the moderately branched/extended, highly fucosylated, and less sialylated natures of the glycoforms of S proteins. Subsequent LMA analysis emphasized the intensive end-capping of glycans by Lewis fucoses, which complemented the glycoproteomic features. These results illustrate the high-resolution glycoproteomic features of the SARS-CoV-2 S protein, contributing to vaccine design and understanding of viral protein synthesis.

    DOI: 10.1021/acs.jproteome.3c00874

    PubMed

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  5. HGA Segment 1: Comprehensive acquisition of human glycan structural information

    Kaji Hiroyuki

    Glycoforum   27 巻 ( 2 ) 頁: A4   2024年4月

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    記述言語:英語   出版者・発行元:SEIKAGAKU CORPORATION  

    DOI: 10.32285/glycoforum.27a4

    CiNii Research

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