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1. Identification of novel hypermethylated or hypomethylated CpG sites and genes associated with anthracycline-induced cardiomyopathy

Author

Purnima Singh, Liting Zhou, Disheet A. Shah, Romina B. Cejas, David K. Crossman, Mariam Jouni, Tarek Magdy, Xuexia Wang, Noha Sharafeldin, Lindsey Hageman, Donald E. McKenna, Steve Horvath, Saro H. Armenian, Frank M. Balis, Douglas S. Hawkins, Frank G. Keller, Melissa M. Hudson, Joseph P. Neglia, A. Kim Ritchey, Jill P. Ginsberg, Wendy Landier, Paul W. Burridge, and Smita Bhatia

Subjects
Medicine, Science
Abstract

Abstract Anthracycline-induced cardiomyopathy is a leading cause of late morbidity in childhood cancer survivors. Aberrant DNA methylation plays a role in de novo cardiovascular disease. Epigenetic processes could play a role in anthracycline-induced cardiomyopathy but remain unstudied. We sought to examine if genome-wide differential methylation at ‘CpG’ sites in peripheral blood DNA is associated with anthracycline-induced cardiomyopathy. This report used participants from a matched case–control study; 52 non-Hispanic White, anthracycline-exposed childhood cancer survivors with cardiomyopathy were matched 1:1 with 52 survivors with no cardiomyopathy. Paired ChAMP (Chip Analysis Methylation Pipeline) with integrated reference-based deconvolution of adult peripheral blood DNA methylation was used to analyze data from Illumina HumanMethylation EPIC BeadChip arrays. An epigenome-wide association study (EWAS) was performed, and the model was adjusted for GrimAge, sex, interaction terms of age at enrollment, chest radiation, age at diagnosis squared, and cardiovascular risk factors (CVRFs: diabetes, hypertension, dyslipidemia). Prioritized genes were functionally validated by gene knockout in human induced pluripotent stem cell cardiomyocytes (hiPSC-CMs) using CRISPR/Cas9 technology. DNA-methylation EPIC array analyses identified 32 differentially methylated probes (DMP: 15 hyper-methylated and 17 hypo-methylated probes) that overlap with 23 genes and 9 intergenic regions. Three hundred and fifty-four differential methylated regions (DMRs) were also identified. Several of these genes are associated with cardiac dysfunction. Knockout of genes EXO6CB, FCHSD2, NIPAL2, and SYNPO2 in hiPSC-CMs increased sensitivity to doxorubicin. In addition, EWAS analysis identified hypo-methylation of probe ‘cg15939386’ in gene RORA to be significantly associated with anthracycline-induced cardiomyopathy. In this genome-wide DNA methylation profile study, we observed significant differences in DNA methylation at the CpG level between anthracycline-exposed childhood cancer survivors with and without cardiomyopathy, implicating differential DNA methylation of certain genes could play a role in pathogenesis of anthracycline-induced cardiomyopathy.

Published
2023
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2. Altered Peripheral Blood Gene Expression in Childhood Cancer Survivors With Anthracycline‐Induced Cardiomyopathy – A COG‐ALTE03N1 Report

Author

Purnima Singh, Disheet A. Shah, Mariam Jouni, Romina B. Cejas, David K. Crossman, Tarek Magdy, Shaowei Qiu, Xuexia Wang, Liting Zhou, Noha Sharafeldin, Lindsey Hageman, Donald E. McKenna, Saro H. Armenian, Frank M. Balis, Douglas S. Hawkins, Frank G. Keller, Melissa M. Hudson, Joseph P. Neglia, A Kim Ritchey, Jill P. Ginsberg, Wendy Landier, Ravi Bhatia, Paul W. Burridge, and Smita Bhatia

Subjects
anthracyclines, cardiomyopathy, childhood cancer survivors, gene expression, peripheral blood, transcriptome, Diseases of the circulatory (Cardiovascular) system, RC666-701
Abstract

Background Anthracycline‐induced cardiomyopathy is a leading cause of premature death in childhood cancer survivors, presenting a need to understand the underlying pathogenesis. We sought to examine differential blood‐based mRNA expression profiles in anthracycline‐exposed childhood cancer survivors with and without cardiomyopathy. Methods and Results We designed a matched case‐control study (Children's Oncology Group‐ALTE03N1) with mRNA sequencing on total RNA from peripheral blood in 40 anthracycline‐exposed survivors with cardiomyopathy (cases) and 64 matched survivors without (controls). DESeq2 identified differentially expressed genes. Ingenuity Pathway Analyses (IPA) and Gene Set Enrichment Analyses determined the potential roles of altered genes in biological pathways. Functional validation was performed by gene knockout in human‐induced pluripotent stem cell‐derived cardiomyocytes using CRISPR/Cas9 (clustered regularly interspaced short palindromic repeats/CRISPR‐associated protein 9) technology. Median age at primary cancer diagnosis for cases and controls was 8.2 and 9.7 years, respectively. Thirty‐six differentially expressed genes with fold change ≥±2 were identified; 35 were upregulated. IPA identified “hepatic fibrosis” and “iron homeostasis” pathways to be significantly modulated by differentially expressed genes, including toxicology functions of myocardial infarction, cardiac damage, and cardiac dilation. Leading edge analysis from Gene Set Enrichment Analyses identified lactate dehydrogenase A (LDHA) and cluster of differentiation 36 (CD36) genes to be significantly upregulated in cases. Interleukin 1 receptor type 1, 2 (IL1R1, IL1R2), and matrix metalloproteinase 8, 9 (MMP8, MMP9) appeared in multiple canonical pathways. LDHA‐knockout human‐induced pluripotent stem cell‐derived cardiomyocytes showed increased sensitivity to doxorubicin. Conclusions We identified differential mRNA expression profiles in peripheral blood of anthracycline‐exposed childhood cancer survivors with and without cardiomyopathy. Upregulation of LDHA and CD36 genes suggests metabolic perturbations in a failing heart. Dysregulation of proinflammatory cytokine receptors IL1R1 and IL1R2 and matrix metalloproteinases, MMP8 and MMP9 indicates structural remodeling that accompanies the clinical manifestation of symptomatic cardiotoxicity.

Published
2023
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4. Analysis of the intracellular traffic of IgG in the context of Down syndrome (trisomy 21)

Author

Javier G. Blanco, Miriam Tamaño-Blanco, and Romina B. Cejas

Subjects
Cell biology, Science, Immunology, Context (language use), Diseases, Biology, Biochemistry, Article, Cell Line, Neonatal Fc receptor, medicine, Animals, Humans, Fibroblast, Messenger RNA, Multidisciplinary, medicine.disease, Molecular biology, Protein Transport, medicine.anatomical_structure, Cell culture, Immunoglobulin G, Medicine, Down Syndrome, Trisomy, Intracellular, Alpha chain
Abstract

Persons with Down syndrome (DS, trisomy 21) have widespread cellular protein trafficking defects. There is a paucity of data describing the intracellular transport of IgG in the context of endosomal-lysosomal alterations linked to trisomy 21. In this study, we analyzed the intracellular traffic of IgG mediated by the human neonatal Fc receptor (FcRn) in fibroblast cell lines with trisomy 21. Intracellular IgG trafficking studies in live cells showed that fibroblasts with trisomy 21 exhibit higher proportion of IgG in lysosomes (~ 10% increase), decreased IgG content in intracellular vesicles (~ 9% decrease), and a trend towards decreased IgG recycling (~ 55% decrease) in comparison to diploid cells. Amyloid-beta precursor protein (APP) overexpression in diploid fibroblasts replicated the increase in IgG sorting to the degradative pathway observed in cells with trisomy 21. The impact of APP on the expression of FCGRT (alpha chain component of FcRn) was investigated by APP knock down and overexpression of the APP protein. APP knock down increased the expression of FCGRT mRNA by ~ 60% in both diploid and trisomic cells. Overexpression of APP in diploid fibroblasts and HepG2 cells resulted in a decrease in FCGRT and FcRn expression. Our results indicate that the intracellular traffic of IgG is altered in cells with trisomy 21. This study lays the foundation for future investigations into the role of FcRn in the context of DS.

Published
2021

5. Contribution of DNA methylation to the expression of FCGRT in human liver and myocardium

Author

Adolfo Quiñones-Lombraña, Daniel C. Ferguson, Romina B. Cejas, Jonathan E. Bard, and Javier G. Blanco

Subjects
0301 basic medicine, Chromatin Immunoprecipitation, Sp1 Transcription Factor, Transcriptional regulatory elements, lcsh:Medicine, Receptors, Fc, Biology, Article, Epigenesis, Genetic, 03 medical and health sciences, 0302 clinical medicine, Albumins, Cell Line, Tumor, Humans, Myocytes, Cardiac, RNA, Messenger, Epigenetics, Promoter Regions, Genetic, lcsh:Science, Transcription factor, DNA methylation, Multidisciplinary, Molecular medicine, Myocardium, Histocompatibility Antigens Class I, lcsh:R, DNA, Methylation, Gene regulation, Cell biology, DNA-Binding Proteins, 030104 developmental biology, Differentially methylated regions, Liver, CpG site, Regulatory sequence, Immunoglobulin G, Hepatocytes, CpG Islands, lcsh:Q, Transcytosis, Chromatin immunoprecipitation, 030217 neurology & neurosurgery, Protein Binding, Transcription Factors
Abstract

FcRn mediates recycling and transcytosis of IgG and albumin in various cell types. The MHC-class-I-like protein of the FcRn heterodimer is encoded by FCGRT. Few determinants of variable FCGRT expression in humans have been identified so far. In this study, we investigated the presence of DNA methylation in regulatory regions of FCGRT in samples of human liver and myocardium tissue, and we examined the impact of FCGRT methylation on FcRn expression in model cell lines. Quantitative DNA methylation analysis of the FCGRT locus revealed differentially methylated regions in DNA from liver and myocardium. Methylation status in individual CpG sites correlated with FCGRT mRNA expression. Data from model cell lines suggest that differential methylation in the −1058 to −587 bp regulatory region of FCGRT contributes to FcRn expression. Chromatin immunoprecipitation assays indicate that CpG site methylation impacts the binding of the methylation sensitive transcription factors Zbtb7a and Sp1. This study provides a foundation to further define the contribution of epigenetic factors during the control of FcRn expression and IgG traffic in human tissues.

Published
2019
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6. Biosynthesis of O-N-acetylgalactosamine glycans in the human cell nucleus

Author

Virginia Lorenz, Fernando J. Irazoqui, Yohana Camila Garay, and Romina B. Cejas

Subjects
0301 basic medicine, Glycan, Glycosylation, Glycoconjugate, Chemical biology, Biochemistry, purl.org/becyt/ford/1 [https], Ciencias Biológicas, 03 medical and health sciences, chemistry.chemical_compound, parasitic diseases, Organelle, Gene expression, BIOSYNTHESIS, Nuclear protein, purl.org/becyt/ford/1.6 [https], NUCLEUS, Molecular Biology, chemistry.chemical_classification, 030102 biochemistry & molecular biology, biology, Glycobiology, Chemistry, POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 3, Cell Biology, Bioquímica y Biología Molecular, carbohydrates (lipids), 030104 developmental biology, biology.protein, lipids (amino acids, peptides, and proteins), CIENCIAS NATURALES Y EXACTAS, O-GALNAC GLYCANS
Abstract

Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported. Here, we examined in detail the initiation of O-GalNAc glycan biosynthesis, representing a novel PTM of nuclear proteins in the nucleus of human cells, with an emphasis on HeLa cells. Using soluble nuclear fractions from purified nuclei, enzymatic assays, fluorescence microscopy, affinity chromatography, MS, and FRET analyses, we identified all factors required for biosynthesis of O-GalNAc glycans in nuclei: the donor substrate (UDP-GalNAc), nuclear polypeptide GalNAc -transferase activity, and a GalNAc transferase (polypeptide GalNAc-T3). Moreover, we identified O-GalNAc glycosylated proteins in the nucleus and present solid evidence for O-GalNAc glycan synthesis in this organelle. The demonstration of O-GalNAc glycosylation of nuclear proteins in mammalian cells reported here has important implications for cell and chemical biology. Fil: Cejas, Romina Beatríz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Lorenz, Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Salud y Ambiente del Litoral. Universidad Nacional del Litoral. Instituto de Salud y Ambiente del Litoral; Argentina Fil: Garay, Yohana Camila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Irazoqui, Fernando Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina

Published
2019
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7. Functional control of polypeptide GalNAc-transferase 3 through an acetylation site in the C-terminal lectin domain

Author

Virginia Lorenz, Gustavo A. Nores, Fernando J. Irazoqui, Romina B. Cejas, and Eric P. Bennett

Subjects
0301 basic medicine, Glycosylation, Otras Ciencias Biológicas, Clinical Biochemistry, Mutant, Cellular homeostasis, K626 SITE, Biochemistry, Ciencias Biológicas, purl.org/becyt/ford/1 [https], 03 medical and health sciences, chemistry.chemical_compound, GLYCOSYLTRANSFERASE, Biosynthesis, C-type lectin, Lectins, Humans, Point Mutation, purl.org/becyt/ford/1.6 [https], Molecular Biology, chemistry.chemical_classification, biology, Acetylation, LECTIN DOMAIN, Enzyme assay, carbohydrates (lipids), 030104 developmental biology, Enzyme, chemistry, biology.protein, N-Acetylgalactosaminyltransferases, CIENCIAS NATURALES Y EXACTAS, O-GALNAC GLYCANS
Abstract

O-GalNAc glycans are important structures in cellular homeostasis. Their biosynthesis is initiated by members of the polypeptide GalNAc-transferase (ppGalNAc-T) enzyme family. Mutations in ppGalNAc-T3 isoform cause diseases (congenital disorders of glycosylation) in humans. The K626 residue located in the C-terminal β-trefoil fold of ppGalNAc-T3 was predicted to be a site with high likelihood of acetylation by CBP/p300 acetyltransferase. We used a site-directed mutagenesis approach to evaluate the role of this acetylation site in biological properties of the enzyme. Two K626 mutants of ppGalNAc-T3 (T3K626Q and T3K626A) had GalNAc-T activities lower than that of wild-type enzyme. Direct and competitive interaction assays revealed that GalNAc recognition by the lectin domain was altered in the mutants. The presence of GlcNAc glycosides affected the interaction of the three enzymes with mucin-derived peptides. In GalNAc-T activity assays, the presence of GlcNAc glycosides significantly inhibited activity of the mutant (T3K626Q) that mimicked acetylation. Our findings, taken together, reveal the crucial role of the K626 residue in the C-terminal β-trefoil fold in biological properties of human ppGalNAc-T3. We propose that acetylated residues on ppGalNAc-T3 function as control points for enzyme activity, and high level of GlcNAc glycosides promote a synergistic regulatory mechanism, leading to a metabolically disordered state. Fil: Lorenz, Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Cejas, Romina Beatríz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Bennett, Eric P.. Universidad de Copenhagen; Dinamarca Fil: Nores, Gustavo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Irazoqui, Fernando Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina

Published
2017
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8. Correction: Biosynthesis of

Author

Romina B, Cejas, Virginia, Lorenz, Yohana C, Garay, and Fernando J, Irazoqui

Subjects
carbohydrates (lipids), parasitic diseases, Glycobiology and Extracellular Matrices, lipids (amino acids, peptides, and proteins)
Abstract

Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of O-linked glycosylation (O-GalNAc) as a PTM of nuclear proteins in the human cell has not been previously reported. Here, we examined in detail the initiation of O-GalNAc glycan biosynthesis, representing a novel PTM of nuclear proteins in the nucleus of human cells, with an emphasis on HeLa cells. Using soluble nuclear fractions from purified nuclei, enzymatic assays, fluorescence microscopy, affinity chromatography, MS, and FRET analyses, we identified all factors required for biosynthesis of O-GalNAc glycans in nuclei: the donor substrate (UDP-GalNAc), nuclear polypeptide GalNAc -transferase activity, and a GalNAc transferase (polypeptide GalNAc-T3). Moreover, we identified O-GalNAc glycosylated proteins in the nucleus and present solid evidence for O-GalNAc glycan synthesis in this organelle. The demonstration of O-GalNAc glycosylation of nuclear proteins in mammalian cells reported here has important implications for cell and chemical biology.

Published
2019

9. Comparative genome-wide DNA methylation analysis in myocardial tissue from donors with and without Down syndrome

Author

Javier G. Blanco, Rachael Hageman-Blair, Song Liu, Jie Wang, and Romina B. Cejas

Subjects
Adult, Epigenomics, Male, 0301 basic medicine, Chromosomes, Human, Pair 21, Biology, Real-Time Polymerase Chain Reaction, Article, Epigenesis, Genetic, Young Adult, 03 medical and health sciences, 0302 clinical medicine, Genetics, medicine, Humans, RNA, Messenger, Child, Gene, Aged, Aged, 80 and over, Reverse Transcriptase Polymerase Chain Reaction, Myocardium, Infant, Sequence Analysis, DNA, General Medicine, Methylation, DNA Methylation, Middle Aged, medicine.disease, genomic DNA, 030104 developmental biology, Differentially methylated regions, CpG site, Genetic Loci, 030220 oncology & carcinogenesis, Core Binding Factor Alpha 2 Subunit, DNA methylation, CpG Islands, Female, Down Syndrome, Chromosome 21, Trisomy
Abstract

Down syndrome (DS, trisomy 21) is the most common major chromosomal aneuploidy compatible with life. The additional whole or partial copy of chromosome 21 results in genome-wide imbalances that drive the complex pathobiology of DS. Differential DNA methylation in the context of trisomy 21 may contribute to the variable architecture of the DS phenotype. The goal of this study was to examine the genomic DNA methylation landscape in myocardial tissue from non-fetal individuals with DS. More than 480,000 unique CpG sites were interrogated in myocardial DNA samples from individuals with (n = 12) and without DS (n = 12) using DNA methylation arrays. A total of 93 highly differentially methylated CpG sites and 16 differentially methylated regions were identified in myocardial DNA from subjects with DS. There were 18 differentially methylated CpG sites in chromosome 21, including 5 highly differentially methylated sites. A CpG site in the RUNX1 locus was differentially methylated in DS myocardium, and linear regression suggests that donors’ age, gender, DS status, and RUNX1 methylation may contribute up to ~51% of the variability in RUNX1 mRNA expression. In DS myocardium, only 58% of the genes overlapping with differentially methylated regions codify for proteins with known functions and 24% are non-coding RNAs. This study provides an initial snapshot on the extent of genome-wide differential methylation in myocardial tissue from persons with DS.

Published
2021
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10. Biosynthesis of

Author

Romina B, Cejas, Virginia, Lorenz, Yohana C, Garay, and Fernando J, Irazoqui

Subjects
Cell Nucleus, Acetylgalactosamine, Glycosylation, Lamin Type B, Polysaccharides, Cell Line, Tumor, Active Transport, Cell Nucleus, Humans, N-Acetylgalactosaminyltransferases, Additions and Corrections
Abstract

Biological functions of nuclear proteins are regulated by post-translational modifications (PTMs) that modulate gene expression and cellular physiology. However, the role of

Published
2018

12. Extrinsic functions of lectin domains in O-N-acetylgalactosamine glycan biosynthesis

Author

Fernando J. Irazoqui, Gustavo A. Nores, Henrik Clausen, Yanina Ditamo, Romina B. Cejas, Virginia Lorenz, Eric P. Bennett, and Maria E. Carrizo

Subjects
0301 basic medicine, Protein Folding, Glycan, Otras Ciencias Biológicas, MUCIN, Protein domain, Glycobiology and Extracellular Matrices, GLYCOPROTEIN BIOSYNTHESIS, CHO Cells, Spodoptera, Biochemistry, GLYCOSYLATION INHIBITOR, Ciencias Biológicas, purl.org/becyt/ford/1 [https], 03 medical and health sciences, symbols.namesake, chemistry.chemical_compound, Cricetulus, Protein Domains, Biosynthesis, Polysaccharides, Cricetinae, Glycosyltransferase, Sf9 Cells, Animals, Drosophila Proteins, Humans, purl.org/becyt/ford/1.6 [https], Molecular Biology, Galactosyltransferase, 030102 biochemistry & molecular biology, biology, Glycobiology, Lectin, Cell Biology, Golgi apparatus, LECTIN, Cell biology, carbohydrates (lipids), Drosophila melanogaster, 030104 developmental biology, GLYCOBIOLOGY, chemistry, biology.protein, symbols, N-Acetylgalactosaminyltransferases, CIENCIAS NATURALES Y EXACTAS, HeLa Cells
Abstract

Glycan biosynthesis occurs mainly in Golgi. Molecular organization and functional regulation of this process are not well understood. We evaluated the extrinsic effect of lectin domains (β-trefoil fold) of polypeptide GalNAc-transferases (ppGalNAc-Ts) on catalytic activity of glycosyltransferases during O-GalNAc glycan biosynthesis. The presence of lectin domain T3lec or T4lec during ppGalNAc-T2 and ppGalNAc-T3 catalytic reaction had a clear inhibitory effect on GalNAc-T activity. Interaction of T3lec or T4lec with ppGalNAc-T2 catalytic domain was not mediated by carbohydrate. T3lec, but not T2lec and T4lec, had a clear activating effect on Drosophila melanogaster core 1 galactosyltransferase enzyme activity and a predominant inhibitory effect on in vivo human core 1 glycan biosynthesis. The regulatory role of the β-trefoil fold of ppGalNAc-Ts in enzymatic activity of glycosyltransferases involved in the O-glycan biosynthesis pathway, described here for the first time, helps clarify the mechanism of biosynthesis of complex biopolymers (such as glycans) that is not template-driven. Fil: Lorenz, Virginia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Ditamo, Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Cejas, Romina Beatríz. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Carrizo Garcia, Maria Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Bennett, Eric P.. Universidad de Copenhagen; Dinamarca Fil: Clausen, Henrik. Universidad de Copenhagen; Dinamarca Fil: Nores, Gustavo Alejandro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Irazoqui, Fernando Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina

Published
2016

13. Arsenic effect on the model crop symbiosis Bradyrhizobium-soybean

Author

Paola S. González, Romina B. Cejas, Elizabeth Agostini, and Melina A. Talano

Subjects
NODULATION, Physiology, SWIMMING, Biotecnología del Medio Ambiente, Swarming (honey bee), chemistry.chemical_element, Plant Science, INGENIERÍAS Y TECNOLOGÍAS, Bradyrhizobium, Plant Root Nodulation, Rhizobia, SOYBEAN, Arsenic, Symbiosis, Metals, Heavy, Botany, HEAVY METALS, Genetics, Bioremediación, Diagnóstico Biotecnológico en Gestión Medioambiental, biology, SYMBIOSIS, Heavy metals, RHIZOREMEDIATION, biology.organism_classification, SWARMING, chemistry, Soybeans
Abstract

Soybean (Glycine max) is often being cultivated in soils with moderate to high arsenic (As) concentrations or under irrigation with As contaminated groundwater. The purpose of this study was to determine the effect of As on soybean germination, development and nodulation in soybean-Bradyrhizobium japonicum E109 symbiosis, as a first-step approach to evaluate the impact of As on soybean production. Semi-hydroponic assays were conducted using soybean seedlings inoculated and non-inoculated with B. japonicum E109 and treated with arsenate or arsenite. Soybean germination and development, at early stage of growth, were significantly reduced from 10 μM arsenate or arsenite. This also was seen for soybean seedlings inoculated with B. japonicum mainly with arsenite where, in addition, the number of effective nodules was reduced, despite that the microorganism tolerated the metalloid. This minor nodulation could be due to a reduced motility (swarming and swimming) of the microorganism in presence of As. Arsenic concentration in roots was about 250-times higher than in shoots. Transference coefficient values indicated that As translocation to aerial parts was low and As accumulated mainly in roots, without significant differences between inoculated and non-inoculated plants. The presence of As restricted soybean–B. japonicum symbiosis and hence, the efficiency of most used commercial inoculants for soybean. Thus, water and/or soils containing As would negatively impact on soybean production, even in plants inoculated with B. japonicum E109. Fil: Talano, Melina Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina Fil: Cejas, Romina Beatríz. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: González, Paola Solange. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina Fil: Agostini, Elizabeth. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina

Published
2012

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