A CRISPR Screen Using Subtilase Cytotoxin Identifies SLC39A9 as a Glycan-Regulating Factor
Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no...
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| Published in | iScience Vol. 15; pp. 407 - 420 |
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| Main Authors | , , , , , , , , |
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Elsevier Inc
31.05.2019
Elsevier |
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| Abstract | Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors.
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•CRISPR knockout screening identified host factors for SubAB-induced cell death•O-glycans as well as N-glycans serve as SubAB receptors•Loss of SLC39A9 as well as loss of KDELR2 and JTB reduces sensitivity to SubAB•SLC39A9 is required for biosynthesis of complex-type N-glycans and core 1 O-glycans
Biological Sciences; Biochemistry; Molecular Biology; Microbiology; Cell Biology |
|---|---|
| AbstractList | Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic
Escherichia coli
strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the
SLC39A9
gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors.
•
CRISPR knockout screening identified host factors for SubAB-induced cell death
•
O-glycans as well as N-glycans serve as SubAB receptors
•
Loss of SLC39A9 as well as loss of KDELR2 and JTB reduces sensitivity to SubAB
•
SLC39A9 is required for biosynthesis of complex-type N-glycans and core 1 O-glycans
Biological Sciences; Biochemistry; Molecular Biology; Microbiology; Cell Biology Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors. [Display omitted] •CRISPR knockout screening identified host factors for SubAB-induced cell death•O-glycans as well as N-glycans serve as SubAB receptors•Loss of SLC39A9 as well as loss of KDELR2 and JTB reduces sensitivity to SubAB•SLC39A9 is required for biosynthesis of complex-type N-glycans and core 1 O-glycans Biological Sciences; Biochemistry; Molecular Biology; Microbiology; Cell Biology Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors. : Biological Sciences; Biochemistry; Molecular Biology; Microbiology; Cell Biology Subject Areas: Biological Sciences, Biochemistry, Molecular Biology, Microbiology, Cell Biology Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors.Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors. Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin recognizes sialoglycans for entry and cleaves an endoplasmic reticulum chaperon, binding immunoglobulin protein, to cause cell death. However, no systematic screening has yet been performed to identify critical host factors. Here, we performed a genome-wide CRISPR/Cas9 knockout screen for SubAB-induced cell death and identified various sialoglycan-related and membrane-trafficking genes. Analysis of glycan-deficient cells demonstrated that not only N-glycans but also O-glycans serve as SubAB receptors. In addition, SLC39A9, which is a predicted zinc transporter, as well as KDELRs and JTB, were required for SubAB to induce maximal cell death. Disruption of the SLC39A9 gene markedly reduced both complex-type N-glycans and core 1 O-glycans, and the O-glycan reduction was attributed to the reduction of core 1 synthase (C1GalT1). These results provide insights into the post-transcriptional regulation of glycosyltransferases by SLC39A9, as well as sialoglycan species as SubAB receptors. |
| Author | Ohnishi, Makoto Kuroda, Makoto Yahiro, Kinnosuke Iwasaki, Norimasa Sekizuka, Tsuyoshi Yamaji, Toshiyuki Hanamatsu, Hisatoshi Hanada, Kentaro Furukawa, Jun-ichi |
| AuthorAffiliation | 4 Pathogen Genomics Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan 7 Department of Molecular Infectiology, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan 1 Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan 3 Department of Gastroenterology and Hepatology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan 5 Department of Orthopaedic Surgery, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan 2 Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo 001-0021, Japan 6 Department of Bacteriology I, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan |
| AuthorAffiliation_xml | – name: 2 Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo 001-0021, Japan – name: 3 Department of Gastroenterology and Hepatology, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan – name: 7 Department of Molecular Infectiology, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan – name: 6 Department of Bacteriology I, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – name: 5 Department of Orthopaedic Surgery, Graduate School of Medicine, Hokkaido University, Sapporo 060-8638, Japan – name: 1 Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – name: 4 Pathogen Genomics Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan |
| Author_xml | – sequence: 1 givenname: Toshiyuki surname: Yamaji fullname: Yamaji, Toshiyuki email: tyamaji@nih.go.jp organization: Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – sequence: 2 givenname: Hisatoshi surname: Hanamatsu fullname: Hanamatsu, Hisatoshi organization: Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo 001-0021, Japan – sequence: 3 givenname: Tsuyoshi surname: Sekizuka fullname: Sekizuka, Tsuyoshi organization: Pathogen Genomics Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – sequence: 4 givenname: Makoto surname: Kuroda fullname: Kuroda, Makoto organization: Pathogen Genomics Center, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – sequence: 5 givenname: Norimasa surname: Iwasaki fullname: Iwasaki, Norimasa organization: Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo 001-0021, Japan – sequence: 6 givenname: Makoto surname: Ohnishi fullname: Ohnishi, Makoto organization: Department of Bacteriology I, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan – sequence: 7 givenname: Jun-ichi surname: Furukawa fullname: Furukawa, Jun-ichi organization: Department of Advanced Clinical Glycobiology, Faculty of Medicine and Graduate School of Medicine, Hokkaido University, Sapporo 001-0021, Japan – sequence: 8 givenname: Kinnosuke surname: Yahiro fullname: Yahiro, Kinnosuke email: yahirok@faculty.chiba-u.jp organization: Department of Molecular Infectiology, Graduate School of Medicine, Chiba University, Chiba 260-8670, Japan – sequence: 9 givenname: Kentaro surname: Hanada fullname: Hanada, Kentaro organization: Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Shinjuku-ku, Tokyo 162-8640, Japan |
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| Snippet | Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin... Subtilase cytotoxin (SubAB) is a virulence factor produced by locus of enterocyte effacement-negative Shiga-toxigenic Escherichia coli strains. The toxin... |
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| Title | A CRISPR Screen Using Subtilase Cytotoxin Identifies SLC39A9 as a Glycan-Regulating Factor |
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