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Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays.

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

McKitrick TR, Hanes MS, Rosenberg CS, Heimburg-Molinaro J, Cooper MD, Herrin BR, Cummings RD.
PMID: 34870812
Methods Mol Biol. 2022;2421:73-89. doi: 10.1007/978-1-0716-1944-5_5.

The jawless vertebrates (lamprey and hagfish) evolved a novel adaptive immune system with many similarities to that found in the jawed vertebrates, including the production of antigen-specific circulating antibodies in response to immunization. However, the jawless vertebrates use leucine-rich...

Cite
McKitrick TR, Hanes MS, Rosenberg CS, et al. Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods Mol Biol. 2022;2421:73-89doi: 10.1007/978-1-0716-1944-5_5.
McKitrick, T. R., Hanes, M. S., Rosenberg, C. S., Heimburg-Molinaro, J., Cooper, M. D., Herrin, B. R., & Cummings, R. D. (2022). Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods in molecular biology (Clifton, N.J.), 242173-89. https://doi.org/10.1007/978-1-0716-1944-5_5
McKitrick, Tanya R, et al. "Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays." Methods in molecular biology (Clifton, N.J.) vol. 2421 (2022): 73-89. doi: https://doi.org/10.1007/978-1-0716-1944-5_5
McKitrick TR, Hanes MS, Rosenberg CS, Heimburg-Molinaro J, Cooper MD, Herrin BR, Cummings RD. Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods Mol Biol. 2022;2421:73-89. doi: 10.1007/978-1-0716-1944-5_5. PMID: 34870812.
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Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines.

Glycobiology

Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK.
PMID: 34350945
Glycobiology. 2021 Dec 18;31(11):1444-1463. doi: 10.1093/glycob/cwab083.

Bladder cancer is the ninth most frequently diagnosed cancer worldwide, and there is a need to develop new biomarkers for staging and prognosis of this disease. Here we report that cell lines derived from low-grade and high-grade bladder cancers...

Cite
Ezeabikwa B, Mondal N, Antonopoulos A, et al. Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021;31(11):1444-1463doi: 10.1093/glycob/cwab083.
Ezeabikwa, B., Mondal, N., Antonopoulos, A., Haslam, S. M., Matsumoto, Y., Martin-Caraballo, M., Lehoux, S., Mandalasi, M., Ishaque, A., Heimburg-Molinaro, J., Cummings, R. D., & Nyame, A. K. (2021). Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology, 31(11), 1444-1463. https://doi.org/10.1093/glycob/cwab083
Ezeabikwa, Bernadette, et al. "Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines." Glycobiology vol. 31,11 (2021): 1444-1463. doi: https://doi.org/10.1093/glycob/cwab083
Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK. Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021 Dec 18;31(11):1444-1463. doi: 10.1093/glycob/cwab083. PMID: 34350945.
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Erratum to: Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies.

Glycobiology

Matsumoto Y, Kudelka MR, Hanes MS, Lehoux S, Dutta S, Jones MB, Stackhouse KA, Cervoni GE, Heimburg-Molinaro J, Smith DF, Ju T, Chaikof EL, Cummings RD.
PMID: 32415964
Glycobiology. 2020 Dec 09;30(12):1015. doi: 10.1093/glycob/cwaa044.

No abstract available.

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Matsumoto Y, Kudelka MR, Hanes MS, et al. Erratum to: Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies. Glycobiology. 2020;30(12):1015doi: 10.1093/glycob/cwaa044.
Matsumoto, Y., Kudelka, M. R., Hanes, M. S., Lehoux, S., Dutta, S., Jones, M. B., Stackhouse, K. A., Cervoni, G. E., Heimburg-Molinaro, J., Smith, D. F., Ju, T., Chaikof, E. L., & Cummings, R. D. (2020). Erratum to: Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies. Glycobiology, 30(12), 1015. https://doi.org/10.1093/glycob/cwaa044
Matsumoto, Yasuyuki, et al. "Erratum to: Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies." Glycobiology vol. 30,12 (2020): 1015. doi: https://doi.org/10.1093/glycob/cwaa044
Matsumoto Y, Kudelka MR, Hanes MS, Lehoux S, Dutta S, Jones MB, Stackhouse KA, Cervoni GE, Heimburg-Molinaro J, Smith DF, Ju T, Chaikof EL, Cummings RD. Erratum to: Identification of Tn antigen O-GalNAc-expressing glycoproteins in human carcinomas using novel anti-Tn recombinant antibodies. Glycobiology. 2020 Dec 09;30(12):1015. doi: 10.1093/glycob/cwaa044. PMID: 32415964; PMCID: PMC7724743.
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Major differences in glycosylation and Fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines.

Glycobiology

Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK.
PMID: 34350945
Glycobiology. 2021 Aug 05; doi: 10.1093/glycob/cwab083. Epub 2021 Aug 05.

Bladder cancer is the ninth most frequently diagnosed cancer worldwide, and there is a need to develop new biomarkers for staging and prognosis of this disease. Here we report that cell lines derived from low-grade and high-grade bladder cancers...

Cite
Ezeabikwa B, Mondal N, Antonopoulos A, et al. Major differences in glycosylation and Fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021;doi: 10.1093/glycob/cwab083.
Ezeabikwa, B., Mondal, N., Antonopoulos, A., Haslam, S. M., Matsumoto, Y., Martin-Caraballo, M., Lehoux, S., Mandalasi, M., Ishaque, A., Heimburg-Molinaro, J., Cummings, R. D., & Nyame, A. K. (2021). Major differences in glycosylation and Fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology, . https://doi.org/10.1093/glycob/cwab083
Ezeabikwa, Bernadette, et al. "Major differences in glycosylation and Fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines." Glycobiology vol. (2021). doi: https://doi.org/10.1093/glycob/cwab083
Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK. Major differences in glycosylation and Fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021 Aug 05; doi: 10.1093/glycob/cwab083. Epub 2021 Aug 05. PMID: 34350945.
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Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins.

Frontiers in chemistry

Gao C, Wei M, McKitrick TR, McQuillan AM, Heimburg-Molinaro J, Cummings RD.
PMID: 31921763
Front Chem. 2019 Dec 13;7:833. doi: 10.3389/fchem.2019.00833. eCollection 2019.

Glycans and glycan binding proteins (GBPs or lectins) are essential components in almost every aspect of immunology. Investigations of the interactions between glycans and GBPs have greatly advanced our understanding of the molecular basis of these fundamental immunological processes....

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Gao C, Wei M, McKitrick TR, et al. Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins. Front Chem. 2019;7:833doi: 10.3389/fchem.2019.00833.
Gao, C., Wei, M., McKitrick, T. R., McQuillan, A. M., Heimburg-Molinaro, J., & Cummings, R. D. (2019). Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins. Frontiers in chemistry, 7833. https://doi.org/10.3389/fchem.2019.00833
Gao, Chao, et al. "Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins." Frontiers in chemistry vol. 7 (2019): 833. doi: https://doi.org/10.3389/fchem.2019.00833
Gao C, Wei M, McKitrick TR, McQuillan AM, Heimburg-Molinaro J, Cummings RD. Glycan Microarrays as Chemical Tools for Identifying Glycan Recognition by Immune Proteins. Front Chem. 2019 Dec 13;7:833. doi: 10.3389/fchem.2019.00833. eCollection 2019. PMID: 31921763; PMCID: PMC6923789.
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Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays.

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

McKitrick TR, Hanes MS, Rosenberg CS, Heimburg-Molinaro J, Cooper MD, Herrin BR, Cummings RD.
PMID: 34870812
Methods Mol Biol. 2022;2421:73-89. doi: 10.1007/978-1-0716-1944-5_5.

The jawless vertebrates (lamprey and hagfish) evolved a novel adaptive immune system with many similarities to that found in the jawed vertebrates, including the production of antigen-specific circulating antibodies in response to immunization. However, the jawless vertebrates use leucine-rich...

Cite
McKitrick TR, Hanes MS, Rosenberg CS, et al. Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods Mol Biol. 2022;2421:73-89doi: 10.1007/978-1-0716-1944-5_5.
McKitrick, T. R., Hanes, M. S., Rosenberg, C. S., Heimburg-Molinaro, J., Cooper, M. D., Herrin, B. R., & Cummings, R. D. (2022). Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods in molecular biology (Clifton, N.J.), 242173-89. https://doi.org/10.1007/978-1-0716-1944-5_5
McKitrick, Tanya R, et al. "Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays." Methods in molecular biology (Clifton, N.J.) vol. 2421 (2022): 73-89. doi: https://doi.org/10.1007/978-1-0716-1944-5_5
McKitrick TR, Hanes MS, Rosenberg CS, Heimburg-Molinaro J, Cooper MD, Herrin BR, Cummings RD. Identification of Glycan-Specific Variable Lymphocyte Receptors Using Yeast Surface Display and Glycan Microarrays. Methods Mol Biol. 2022;2421:73-89. doi: 10.1007/978-1-0716-1944-5_5. PMID: 34870812.
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Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity.

Science advances

Gao C, Stavenhagen K, Eckmair B, McKitrick TR, Mehta AY, Matsumoto Y, McQuillan AM, Hanes MS, Eris D, Baker KJ, Jia N, Wei M, Heimburg-Molinaro J, Ernst B, Cummings RD.
PMID: 34108208
Sci Adv. 2021 Jun 09;7(24). doi: 10.1126/sciadv.abf6834. Print 2021 Jun.

The recognition of oligomannose-type glycans in innate and adaptive immunity is elusive due to multiple closely related isomeric glycan structures. To explore the functions of oligomannoses, we developed a multifaceted approach combining mass spectrometry assignments of oligomannose substructures and...

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Gao C, Stavenhagen K, Eckmair B, et al. Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity. Sci Adv. 2021;7(24)doi: 10.1126/sciadv.abf6834.
Gao, C., Stavenhagen, K., Eckmair, B., McKitrick, T. R., Mehta, A. Y., Matsumoto, Y., McQuillan, A. M., Hanes, M. S., Eris, D., Baker, K. J., Jia, N., Wei, M., Heimburg-Molinaro, J., Ernst, B., & Cummings, R. D. (2021). Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity. Science advances, 7(24), . https://doi.org/10.1126/sciadv.abf6834
Gao, Chao, et al. "Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity." Science advances vol. 7,24 (2021). doi: https://doi.org/10.1126/sciadv.abf6834
Gao C, Stavenhagen K, Eckmair B, McKitrick TR, Mehta AY, Matsumoto Y, McQuillan AM, Hanes MS, Eris D, Baker KJ, Jia N, Wei M, Heimburg-Molinaro J, Ernst B, Cummings RD. Differential recognition of oligomannose isomers by glycan-binding proteins involved in innate and adaptive immunity. Sci Adv. 2021 Jun 09;7(24). doi: 10.1126/sciadv.abf6834. Print 2021 Jun. PMID: 34108208; PMCID: PMC8189592.
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Glycoconjugates in host-helminth interactions.

Frontiers in immunology

Prasanphanich NS, Mickum ML, Heimburg-Molinaro J, Cummings RD.
PMID: 24009607
Front Immunol. 2013 Aug 28;4:240. doi: 10.3389/fimmu.2013.00240. eCollection 2013.

Helminths are multicellular parasitic worms that comprise a major class of human pathogens and cause an immense amount of suffering worldwide. Helminths possess an abundance of complex and unique glycoconjugates that interact with both the innate and adaptive arms...

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Prasanphanich NS, Mickum ML, Heimburg-Molinaro J, et al. Glycoconjugates in host-helminth interactions. Front Immunol. 2013;4:240doi: 10.3389/fimmu.2013.00240.
Prasanphanich, N. S., Mickum, M. L., Heimburg-Molinaro, J., & Cummings, R. D. (2013). Glycoconjugates in host-helminth interactions. Frontiers in immunology, 4240. https://doi.org/10.3389/fimmu.2013.00240
Prasanphanich, Nina Salinger, et al. "Glycoconjugates in host-helminth interactions." Frontiers in immunology vol. 4 (2013): 240. doi: https://doi.org/10.3389/fimmu.2013.00240
Prasanphanich NS, Mickum ML, Heimburg-Molinaro J, Cummings RD. Glycoconjugates in host-helminth interactions. Front Immunol. 2013 Aug 28;4:240. doi: 10.3389/fimmu.2013.00240. eCollection 2013. PMID: 24009607; PMCID: PMC3755266.
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Natural and Synthetic Sialylated Glycan Microarrays and Their Applications.

Frontiers in molecular biosciences

McQuillan AM, Byrd-Leotis L, Heimburg-Molinaro J, Cummings RD.
PMID: 31572731
Front Mol Biosci. 2019 Sep 13;6:88. doi: 10.3389/fmolb.2019.00088. eCollection 2019.

This focused chapter serves as a short survey of glycan microarrays that are available with sialylated glycans, including both defined and shotgun arrays, their generation, and their utility in studying differential binding interactions to sialylated compounds, highlighting N-glycolyl (Gc)...

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McQuillan AM, Byrd-Leotis L, Heimburg-Molinaro J, et al. Natural and Synthetic Sialylated Glycan Microarrays and Their Applications. Front Mol Biosci. 2019;6:88doi: 10.3389/fmolb.2019.00088.
McQuillan, A. M., Byrd-Leotis, L., Heimburg-Molinaro, J., & Cummings, R. D. (2019). Natural and Synthetic Sialylated Glycan Microarrays and Their Applications. Frontiers in molecular biosciences, 688. https://doi.org/10.3389/fmolb.2019.00088
McQuillan, Alyssa M, et al. "Natural and Synthetic Sialylated Glycan Microarrays and Their Applications." Frontiers in molecular biosciences vol. 6 (2019): 88. doi: https://doi.org/10.3389/fmolb.2019.00088
McQuillan AM, Byrd-Leotis L, Heimburg-Molinaro J, Cummings RD. Natural and Synthetic Sialylated Glycan Microarrays and Their Applications. Front Mol Biosci. 2019 Sep 13;6:88. doi: 10.3389/fmolb.2019.00088. eCollection 2019. PMID: 31572731; PMCID: PMC6753469.
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Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines.

Glycobiology

Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK.
PMID: 34350945
Glycobiology. 2021 Dec 18;31(11):1444-1463. doi: 10.1093/glycob/cwab083.

Bladder cancer is the ninth most frequently diagnosed cancer worldwide, and there is a need to develop new biomarkers for staging and prognosis of this disease. Here we report that cell lines derived from low-grade and high-grade bladder cancers...

Cite
Ezeabikwa B, Mondal N, Antonopoulos A, et al. Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021;31(11):1444-1463doi: 10.1093/glycob/cwab083.
Ezeabikwa, B., Mondal, N., Antonopoulos, A., Haslam, S. M., Matsumoto, Y., Martin-Caraballo, M., Lehoux, S., Mandalasi, M., Ishaque, A., Heimburg-Molinaro, J., Cummings, R. D., & Nyame, A. K. (2021). Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology, 31(11), 1444-1463. https://doi.org/10.1093/glycob/cwab083
Ezeabikwa, Bernadette, et al. "Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines." Glycobiology vol. 31,11 (2021): 1444-1463. doi: https://doi.org/10.1093/glycob/cwab083
Ezeabikwa B, Mondal N, Antonopoulos A, Haslam SM, Matsumoto Y, Martin-Caraballo M, Lehoux S, Mandalasi M, Ishaque A, Heimburg-Molinaro J, Cummings RD, Nyame AK. Major differences in glycosylation and fucosyltransferase expression in low-grade versus high-grade bladder cancer cell lines. Glycobiology. 2021 Dec 18;31(11):1444-1463. doi: 10.1093/glycob/cwab083. PMID: 34350945.
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Tools for generating and analyzing glycan microarray data.

Beilstein journal of organic chemistry

Mehta AY, Heimburg-Molinaro J, Cummings RD.
PMID: 32983270
Beilstein J Org Chem. 2020 Sep 10;16:2260-2271. doi: 10.3762/bjoc.16.187. eCollection 2020.

Glycans are one of the major biological polymers found in the mammalian body. They play a vital role in a number of physiologic and pathologic conditions. Glycan microarrays allow a plethora of information to be obtained on protein-glycan binding...

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Mehta AY, Heimburg-Molinaro J, Cummings RD. Tools for generating and analyzing glycan microarray data. Beilstein J Org Chem. 2020;16:2260-2271doi: 10.3762/bjoc.16.187.
Mehta, A. Y., Heimburg-Molinaro, J., & Cummings, R. D. (2020). Tools for generating and analyzing glycan microarray data. Beilstein journal of organic chemistry, 162260-2271. https://doi.org/10.3762/bjoc.16.187
Mehta, Akul Y, et al. "Tools for generating and analyzing glycan microarray data." Beilstein journal of organic chemistry vol. 16 (2020): 2260-2271. doi: https://doi.org/10.3762/bjoc.16.187
Mehta AY, Heimburg-Molinaro J, Cummings RD. Tools for generating and analyzing glycan microarray data. Beilstein J Org Chem. 2020 Sep 10;16:2260-2271. doi: 10.3762/bjoc.16.187. eCollection 2020. PMID: 32983270; PMCID: PMC7492694.
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Derivatization of free natural glycans for incorporation onto glycan arrays: derivatizing glycans on the microscale for microarray and other applications (ms# CP-10-0194).

Current protocols in chemical biology

Song X, Heimburg-Molinaro J, Smith DF, Cummings RD.
PMID: 22022660
Curr Protoc Chem Biol. 2011 Apr 01;3(2):53-63. doi: 10.1002/9780470559277.ch100194.

Nature possesses an unlimited number and source of biologically-relevant natural glycans, many of which are too complicated to synthesize in the laboratory. To capitalize on the naturally-occurring plethora of glycans, we have developed a method to fluorescently tag the...

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Song X, Heimburg-Molinaro J, Smith DF, et al. Derivatization of free natural glycans for incorporation onto glycan arrays: derivatizing glycans on the microscale for microarray and other applications (ms# CP-10-0194). Curr Protoc Chem Biol. 2011;3(2):53-63doi: 10.1002/9780470559277.ch100194.
Song, X., Heimburg-Molinaro, J., Smith, D. F., & Cummings, R. D. (2011). Derivatization of free natural glycans for incorporation onto glycan arrays: derivatizing glycans on the microscale for microarray and other applications (ms# CP-10-0194). Current protocols in chemical biology, 3(2), 53-63. https://doi.org/10.1002/9780470559277.ch100194
Song, Xuezheng, et al. "Derivatization of free natural glycans for incorporation onto glycan arrays: derivatizing glycans on the microscale for microarray and other applications (ms# CP-10-0194)." Current protocols in chemical biology vol. 3,2 (2011): 53-63. doi: https://doi.org/10.1002/9780470559277.ch100194
Song X, Heimburg-Molinaro J, Smith DF, Cummings RD. Derivatization of free natural glycans for incorporation onto glycan arrays: derivatizing glycans on the microscale for microarray and other applications (ms# CP-10-0194). Curr Protoc Chem Biol. 2011 Apr 01;3(2):53-63. doi: 10.1002/9780470559277.ch100194. PMID: 22022660; PMCID: PMC3196601.
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