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Article: Regeneration of Free Reducing Glycans from Reductive Amination-Tagged Glycans by Oxone

Zhang, Qing / Wang, Shuaishuai / Li, Zhonghua / Lasanajak, Yi / Li, Lei / Song, Xuezheng

Journal of organic chemistry. 2022 Feb. 10, v. 87, no. 5

2022

Abstract: Glycans are usually fluorescently tagged by reductive amination for analytic tools. However, free reducing glycan regeneration is sometimes important and necessary for further structural or functional studies. Here, we introduce a new method for ... ...

Abstract	Glycans are usually fluorescently tagged by reductive amination for analytic tools. However, free reducing glycan regeneration is sometimes important and necessary for further structural or functional studies. Here, we introduce a new method for efficiently removing fluorescent tags from glycoconjugates by a simple treatment with Oxone. This method is proven to be fast and general after being tested on a series of common saccharides and widely used tags. We successfully achieved N-glycopeptide synthesis by using the regenerated glycans.
Keywords	amination ; fluorescence ; glycoconjugates ; organic chemistry ; polysaccharides
Language	English
Dates of publication	2022-0210
Size	p. 3736-3740.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	123490-0
ISSN	1520-6904 ; 0022-3263
ISSN (online)	1520-6904
ISSN	0022-3263
DOI	10.1021/acs.joc.1c02709
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Serum glycomic profile as a predictive biomarker of recurrence in patients with differentiated thyroid cancer.

Kudelka, Matthew R / Lasanajak, Yi / Smith, David F / Song, Xuezheng / Hossain, Mohammad S / Owonikoko, Taofeek K

Cancer medicine

2022 Volume 12, Issue 6, Page(s) 6768–6777

Abstract: Purpose: Thyroid cancer recurrence following curative thyroidectomy is associated with increased morbidity and mortality, but current surveillance strategies are inadequate for early detection. Prior studies indicate that tissue glycosylation is altered ...

Abstract	Purpose: Thyroid cancer recurrence following curative thyroidectomy is associated with increased morbidity and mortality, but current surveillance strategies are inadequate for early detection. Prior studies indicate that tissue glycosylation is altered in thyroid cancer, but the utility of serum glycosylation in thyroid cancer surveillance remains unexplored. We therefore assessed the potential utility of altered serum glycomic profile as a tumor-specific target for disease surveillance in recurrent thyroid cancer. Experimental design: We employed banked serum samples from patients with recurrent thyroid cancer post thyroidectomy and healthy controls. N-glycans were enzymatically released from serum glycoproteins, labeled via permethylation, and analyzed by MALDI-TOF mass spectrometry. Global level and specific subtypes of glycan structures were compared between patients and controls. Results: We evaluated 28 independent samples from 13 patients with cancer recurrence and 15 healthy controls. Global features of glycosylation, including N-glycan class and terminal glycan modifications were similar between groups, but three of 35 individual glycans showed significant differences. The three glycans were biosynthetically related biantennary core fucosylated N-glycans that only varied by the degree of galactosylation (G0F, G1F, and G2F; G: galactose, F: fucose). The ratio of G0F:G1F that captures reduced galactosylation was observed in patients samples but not in healthy controls (p = 0.004) and predicted thyroid cancer recurrence (AUC = 0.82, CI 95% = 0.64-0.99). Conclusions: Altered N-glycomic profile was associated with thyroid cancer recurrence. This serum-based biomarker would be useful as an effective surveillance tool to improve the care and prognosis of thyroid cancer after prospective validation.
MeSH term(s)	Humans ; Glycomics/methods ; Neoplasm Recurrence, Local ; Biomarkers ; Adenocarcinoma ; Polysaccharides ; Thyroid Neoplasms/diagnosis ; Thyroid Neoplasms/surgery ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Biomarkers ; Polysaccharides
Language	English
Publishing date	2022-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2659751-2
ISSN	2045-7634 ; 2045-7634
ISSN (online)	2045-7634
ISSN	2045-7634
DOI	10.1002/cam4.5465
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Regeneration of Free Reducing Glycans from Reductive Amination-Tagged Glycans by Oxone.

Zhang, Qing / Wang, Shuaishuai / Li, Zhonghua / Lasanajak, Yi / Li, Lei / Song, Xuezheng

The Journal of organic chemistry

2022 Volume 87, Issue 5, Page(s) 3736–3740

Abstract	Glycans are usually fluorescently tagged by reductive amination for analytic tools. However, free reducing glycan regeneration is sometimes important and necessary for further structural or functional studies. Here, we introduce a new method for efficiently removing fluorescent tags from glycoconjugates by a simple treatment with Oxone. This method is proven to be fast and general after being tested on a series of common saccharides and widely used tags. We successfully achieved
MeSH term(s)	Amination ; Glycoconjugates ; Polysaccharides/chemistry ; Regeneration ; Sulfuric Acids
Chemical Substances	Glycoconjugates ; Polysaccharides ; Sulfuric Acids ; potassium peroxymonosulfuric acid (HL6A2XXU5D)
Language	English
Publishing date	2022-02-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	123490-0
ISSN	1520-6904 ; 0022-3263
ISSN (online)	1520-6904
ISSN	0022-3263
DOI	10.1021/acs.joc.1c02709
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Article ; Online: Novel fold of rotavirus glycan-binding domain predicted by AlphaFold2 and determined by X-ray crystallography.

Hu, Liya / Salmen, Wilhelm / Sankaran, Banumathi / Lasanajak, Yi / Smith, David F / Crawford, Sue E / Estes, Mary K / Prasad, B V Venkataram

Communications biology

2022 Volume 5, Issue 1, Page(s) 419

Abstract: The VP8* domain of spike protein VP4 in group A and C rotaviruses, which cause epidemic gastroenteritis in children, exhibits a conserved galectin-like fold for recognizing glycans during cell entry. In group B rotavirus, which causes significant ... ...

Abstract	The VP8* domain of spike protein VP4 in group A and C rotaviruses, which cause epidemic gastroenteritis in children, exhibits a conserved galectin-like fold for recognizing glycans during cell entry. In group B rotavirus, which causes significant diarrheal outbreaks in adults, the VP8* domain (VP8B) surprisingly lacks sequence similarity with VP8 of group A or group C rotavirus. Here, by using the recently developed AlphaFold2 for ab initio structure prediction and validating the predicted model by determining a 1.3-Å crystal structure, we show that VP8B exhibits a novel fold distinct from the galectin fold. This fold with a β-sheet clasping an α-helix represents a new fold for glycan recognition based on glycan array screening, which shows that VP8B recognizes glycans containing N-acetyllactosamine moiety. Although uncommon, our study illustrates how evolution can incorporate structurally distinct folds with similar functionality in a homologous protein within the same virus genus.
MeSH term(s)	Capsid Proteins/metabolism ; Child ; Crystallography, X-Ray ; Galectins/metabolism ; Humans ; Polysaccharides/metabolism ; Rotavirus/chemistry ; Rotavirus/metabolism
Chemical Substances	Capsid Proteins ; Galectins ; Polysaccharides
Language	English
Publishing date	2022-05-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-022-03357-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Limited Neonatal Carbohydrate-Specific Antibody Repertoire Consecutive to Partial Prenatal Transfer of Maternal Antibodies.

Kappler, Katharina / Restin, Tanja / Lasanajak, Yi / Smith, David F / Bassler, Dirk / Hennet, Thierry

Frontiers in immunology

2020 Volume 11, Page(s) 573629

Abstract: Despite the prominence of carbohydrate-specific antibodies in human sera, data on their emergence and antigen specificities are limited. Whereas maternal IgG are transferred prenatally to the fetal circulation, IgM present in cord blood originate from ... ...

Abstract	Despite the prominence of carbohydrate-specific antibodies in human sera, data on their emergence and antigen specificities are limited. Whereas maternal IgG are transferred prenatally to the fetal circulation, IgM present in cord blood originate from fetal B lymphocytes. Considering the limited exposure of the fetus to foreign antigens, we assessed the repertoire of carbohydrate-specific antibodies in human cord blood and matched maternal blood samples using glycan arrays. Carbohydrate-specific IgM was absent in cord blood, whereas low cord blood IgG reactivity to glycans was detectable. Comparing IgG reactivities of matched pairs, we observed a general lack of correlation in the antigen specificity of IgG from cord blood and maternal blood due to a selective exclusion of most carbohydrate-specific IgG from maternofetal transfer. Given the importance of intestinal bacteria in inducing carbohydrate-specific antibodies, we analyzed global antibody specificities toward commensal bacteria. Similar IgG reactivities to specific
MeSH term(s)	Antibody Specificity ; Antigens ; Bacteroides/immunology ; Carbohydrates/immunology ; Female ; Fetal Blood/immunology ; Glycosylation ; Histocompatibility, Maternal-Fetal ; Humans ; Immunoglobulin G/blood ; Immunoglobulin M/blood ; Infant, Newborn ; Maternal-Fetal Exchange ; Placental Circulation ; Pregnancy
Chemical Substances	Antigens ; Carbohydrates ; Immunoglobulin G ; Immunoglobulin M
Language	English
Publishing date	2020-10-14
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2606827-8
ISSN	1664-3224 ; 1664-3224
ISSN (online)	1664-3224
ISSN	1664-3224
DOI	10.3389/fimmu.2020.573629
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: O

Zhang, Ying / Zhu, Yuyang / Lasanajak, Yi / Smith, David F / Song, Xuezheng

SLAS technology

2020 Volume 25, Issue 4, Page(s) 388–396

Abstract: Glycoscience has been recognized as an important area in biomedical research. Currently, a major obstacle for glycoscience study is the lack of diverse, biomedically relevant, and complex glycans in quantities sufficient for exploring their structural ... ...

Abstract	Glycoscience has been recognized as an important area in biomedical research. Currently, a major obstacle for glycoscience study is the lack of diverse, biomedically relevant, and complex glycans in quantities sufficient for exploring their structural and functional aspects. Complementary to chemoenzymatic synthesis, natural glycans could serve as a great source of biomedically relevant glycans if they are available in sufficient quantities. We have recently developed oxidative release of natural glycans (ORNG) for large-scale release of
MeSH term(s)	Acetylation ; Chromatography, High Pressure Liquid ; Hydroxylamines/chemistry ; Methylation ; Milk, Human/chemistry ; Oligosaccharides/chemistry ; Oxidation-Reduction ; Polysaccharides/chemistry ; Polysaccharides/isolation & purification ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Chemical Substances	Hydroxylamines ; Oligosaccharides ; Polysaccharides ; benzyloxyamine (622-33-3) ; lacto-N-neotetraose (BY63N40B1L)
Language	English
Publishing date	2020-01-21
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2900310-6
ISSN	2472-6311 ; 2472-6303
ISSN (online)	2472-6311
ISSN	2472-6303
DOI	10.1177/2472630319898150
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Increased Antibody Response to Fucosylated Oligosaccharides and Fucose-Carrying

Kappler, Katharina / Lasanajak, Yi / Smith, David F / Opitz, Lennart / Hennet, Thierry

Frontiers in microbiology

2020 Volume 11, Page(s) 1553

Abstract: Inflammatory bowel disease is associated with intestinal dysbiosis and with elevated antibody production toward microbial epitopes. The underlying processes linking the gut microbiota with inflammation are still unclear. Considering the constant ... ...

Abstract	Inflammatory bowel disease is associated with intestinal dysbiosis and with elevated antibody production toward microbial epitopes. The underlying processes linking the gut microbiota with inflammation are still unclear. Considering the constant induction of antibodies by gut microbial glycans, the aim of this study was to address whether the repertoire of carbohydrate-specific antibodies is altered in Crohn's disease or ulcerative colitis. IgG and IgM reactivities to oligosaccharides representative of mucosal glycans were tested in blood serum from 20 healthy control subjects, 17 ulcerative colitis patients, and 23 Crohn's disease patients using glycan arrays. An increased IgG and IgM reactivity toward fucosylated oligosaccharides was detected in Crohn's disease but not in ulcerative colitis. To address the antibody reactivity to the gut microbiota, IgG binding to members of a complex intestinal microbiota was measured and observed to be increased in sera of patients with Crohn's disease. Based on the elevated reactivity to fucosylated oligosaccharides, gut bacteria were tested for recognition by the fucose-binding
Language	English
Publishing date	2020-07-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2020.01553
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Article ; Online: Structural analysis of carbohydrate binding by the macrophage mannose receptor CD206.

Feinberg, Hadar / Jégouzo, Sabine A F / Lasanajak, Yi / Smith, David F / Drickamer, Kurt / Weis, William I / Taylor, Maureen E

The Journal of biological chemistry

2021 Volume 296, Page(s) 100368

Abstract: The human mannose receptor expressed on macrophages and hepatic endothelial cells scavenges released lysosomal enzymes, glycopeptide fragments of collagen, and pathogenic microorganisms and thus reduces damage following tissue injury. The receptor binds ... ...

Abstract	The human mannose receptor expressed on macrophages and hepatic endothelial cells scavenges released lysosomal enzymes, glycopeptide fragments of collagen, and pathogenic microorganisms and thus reduces damage following tissue injury. The receptor binds mannose, fucose, or N-acetylglucosamine (GlcNAc) residues on these targets. C-type carbohydrate-recognition domain 4 (CRD4) of the receptor contains the site for Ca
MeSH term(s)	Binding Sites ; Carbohydrate Metabolism/physiology ; Carbohydrates/chemistry ; Carbohydrates/physiology ; Crystallography, X-Ray/methods ; Disaccharides/metabolism ; Glycopeptides/metabolism ; Glycoproteins/metabolism ; Humans ; Lectins, C-Type/metabolism ; Lectins, C-Type/physiology ; Ligands ; Macrophages/metabolism ; Mannose/metabolism ; Mannose Receptor ; Mannose-Binding Lectins/metabolism ; Mannose-Binding Lectins/physiology ; Membrane Glycoproteins/metabolism ; Membrane Glycoproteins/physiology ; Monosaccharides/metabolism ; Oligosaccharides/metabolism ; Polysaccharides/metabolism ; Protein Conformation ; Receptors, Cell Surface/metabolism ; Receptors, Cell Surface/physiology ; Receptors, Immunologic/metabolism ; Receptors, Immunologic/physiology
Chemical Substances	Carbohydrates ; Disaccharides ; Glycopeptides ; Glycoproteins ; Lectins, C-Type ; Ligands ; MRC1 protein, human ; Mannose Receptor ; Mannose-Binding Lectins ; Membrane Glycoproteins ; Monosaccharides ; Oligosaccharides ; Polysaccharides ; Receptors, Cell Surface ; Receptors, Immunologic ; Mannose (PHA4727WTP)
Language	English
Publishing date	2021-02-02
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2021.100368
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Article ; Online: SARS-CoV-2 and other coronaviruses bind to phosphorylated glycans from the human lung.

Byrd-Leotis, Lauren / Lasanajak, Yi / Bowen, Thomas / Baker, Kelly / Song, Xuezheng / Suthar, Mehul S / Cummings, Richard D / Steinhauer, David A

Virology

2021 Volume 562, Page(s) 142–148

Abstract: SARS-CoV, MERS-CoV, and potentially SARS-CoV-2 emerged as novel human coronaviruses following cross-species transmission from animal hosts. Although the receptor binding characteristics of human coronaviruses are well documented, the role of carbohydrate ...

Abstract	SARS-CoV, MERS-CoV, and potentially SARS-CoV-2 emerged as novel human coronaviruses following cross-species transmission from animal hosts. Although the receptor binding characteristics of human coronaviruses are well documented, the role of carbohydrate binding in addition to recognition of proteinaceous receptors has not been fully explored. Using natural glycan microarray technology, we identified N-glycans in the human lung that are recognized by various human and animal coronaviruses. All viruses tested, including SARS-CoV-2, bound strongly to a range of phosphorylated, high mannose N-glycans and to a very specific set of sialylated structures. Examination of two linked strains, human CoV OC43 and bovine CoV Mebus, reveals shared binding to the sialic acid form Neu5Gc (not found in humans), supporting the evidence for cross-species transmission of the bovine strain. Our findings, revealing robust recognition of lung glycans, suggest that these receptors could play a role in the initial stages of coronavirus attachment and entry.
MeSH term(s)	Animals ; COVID-19/virology ; Cattle ; Host Microbial Interactions/physiology ; Humans ; Lung/metabolism ; Mannose/chemistry ; Middle East Respiratory Syndrome Coronavirus/metabolism ; Middle East Respiratory Syndrome Coronavirus/physiology ; N-Acetylneuraminic Acid/chemistry ; Phosphorylation ; Polysaccharides/metabolism ; Protein Array Analysis ; Protein Binding ; SARS-CoV-2/metabolism ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/chemistry ; Spike Glycoprotein, Coronavirus/physiology
Chemical Substances	Polysaccharides ; Spike Glycoprotein, Coronavirus ; N-Acetylneuraminic Acid (GZP2782OP0) ; Mannose (PHA4727WTP)
Language	English
Publishing date	2021-07-23
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.07.012
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Article: SARS-CoV-2 and other coronaviruses bind to phosphorylated glycans from the human lung

Byrd-Leotis, Lauren / Lasanajak, Yi / Bowen, Thomas / Baker, Kelly / Song, Xuezheng / Suthar, Mehul S. / Cummings, Richard D. / Steinhauer, David A.

Virology. 2021 Oct., v. 562

2021

Abstract	SARS-CoV, MERS-CoV, and potentially SARS-CoV-2 emerged as novel human coronaviruses following cross-species transmission from animal hosts. Although the receptor binding characteristics of human coronaviruses are well documented, the role of carbohydrate binding in addition to recognition of proteinaceous receptors has not been fully explored. Using natural glycan microarray technology, we identified N-glycans in the human lung that are recognized by various human and animal coronaviruses. All viruses tested, including SARS-CoV-2, bound strongly to a range of phosphorylated, high mannose N-glycans and to a very specific set of sialylated structures. Examination of two linked strains, human CoV OC43 and bovine CoV Mebus, reveals shared binding to the sialic acid form Neu5Gc (not found in humans), supporting the evidence for cross-species transmission of the bovine strain. Our findings, revealing robust recognition of lung glycans, suggest that these receptors could play a role in the initial stages of coronavirus attachment and entry.
Keywords	Coronavirus infections ; Severe acute respiratory syndrome coronavirus 2 ; cattle ; humans ; lungs ; mannose ; microarray technology ; polysaccharides ; sialic acid ; virology
Language	English
Dates of publication	2021-10
Size	p. 142-148.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/j.virol.2021.07.012
Database	NAL-Catalogue (AGRICOLA)

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