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2. Mucin O-glycans are natural inhibitors of Candida albicans pathogenicity

Author

Takagi, Julie, Aoki, Kazuhiro, Turner, Bradley S, Lamont, Sabrina, Lehoux, Sylvain, Kavanaugh, Nicole, Gulati, Megha, Valle Arevalo, Ashley, Lawrence, Travis J, Kim, Colin Y, Bakshi, Bhavya, Ishihara, Mayumi, Nobile, Clarissa J, Cummings, Richard D, Wozniak, Daniel J, Tiemeyer, Michael, Hevey, Rachel, and Ribbeck, Katharina

Subjects
Infectious Diseases, Rare Diseases, Lung, Cystic Fibrosis, 2.1 Biological and endogenous factors, Aetiology, 2.2 Factors relating to the physical environment, Infection, Candida albicans, Fucose, Mucins, Polysaccharides, Virulence, Medicinal and Biomolecular Chemistry, Biochemistry and Cell Biology, Biochemistry & Molecular Biology
Abstract

Mucins are large gel-forming polymers inside the mucus barrier that inhibit the yeast-to-hyphal transition of Candida albicans, a key virulence trait of this important human fungal pathogen. However, the molecular motifs in mucins that inhibit filamentation remain unclear despite their potential for therapeutic interventions. Here, we determined that mucins display an abundance of virulence-attenuating molecules in the form of mucin O-glycans. We isolated and cataloged >100 mucin O-glycans from three major mucosal surfaces and established that they suppress filamentation and related phenotypes relevant to infection, including surface adhesion, biofilm formation and cross-kingdom competition between C. albicans and the bacterium Pseudomonas aeruginosa. Using synthetic O-glycans, we identified three structures (core 1, core 1 + fucose and core 2 + galactose) that are sufficient to inhibit filamentation with potency comparable to the complex O-glycan pool. Overall, this work identifies mucin O-glycans as host molecules with untapped therapeutic potential to manage fungal pathogens.

Published
2022

3. Galectin-4 Antimicrobial Activity Primarily Occurs Through its C-Terminal Domain

Author

Jan, Hau-Ming, Wu, Shang-Chuen, Stowell, Carter J., Vallecillo-Zúniga, Mary L., Paul, Anu, Patel, Kashyap R., Muthusamy, Sasikala, Lin, Hsien-Ya, Ayona, Diyoly, Jajosky, Ryan Philip, Varadkar, Samata P., Nakahara, Hirotomo, Chan, Rita, Bhave, Devika, Lane, William J., Yeung, Melissa Y., Hollenhorst, Marie A., Rakoff-Nahoum, Seth, Cummings, Richard D., Arthur, Connie M., and Stowell, Sean R.

Published
2024
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6. Pilot Study Showing Feasibility of Phosphoproteomic Profiling of Pathway-Level Molecular Alterations in Barrett’s Esophagus

Author

Moore, Jarrod, Hekman, Ryan, Blum, Benjamin C, Lawton, Matthew, Lehoux, Sylvain, Stachler, Matthew, Pleskow, Douglas, Sawhney, Mandeep S, Cummings, Richard D, Emili, Andrew, and Qureshi, Alia

Subjects
Biochemistry and Cell Biology, Biological Sciences, Rare Diseases, Human Genome, Clinical Research, Digestive Diseases, Genetics, Cancer, 2.1 Biological and endogenous factors, Aetiology, Good Health and Well Being, Barrett Esophagus, Disease Progression, Feasibility Studies, Humans, Pilot Projects, Proteomics, pre-cancerous lesion, biopsy, systems biology, mass spectrometry, disease signature
Abstract

(1) Background: Barrett's esophagus is a major risk factor for esophageal adenocarcinoma. In this pilot study, we employed precision mass spectrometry to map global (phospho)protein perturbations in Barrett's esophagus lesions and adjacent normal tissue to glean insights into disease progression. (2) Methods: Biopsies were collected from two small but independent cohorts. Comparative analyses were performed between Barrett's esophagus samples and adjacent matched (normal) tissues from patients with known pathology, while specimens from healthy patients served as additional controls. (3) Results: We identified and quantified 6810 proteins and 6395 phosphosites in the discovery cohort, revealing hundreds of statistically significant differences in protein abundances and phosphorylation states. We identified a robust proteomic signature that accurately classified the disease status of samples from the independent patient cohorts. Pathway-level analysis of the phosphoproteomic profiles revealed the dysregulation of specific cellular processes, including DNA repair, in Barrett's esophagus relative to paired controls. Comparative analysis with previously published transcriptomic profiles provided independent evidence in support of these preliminary findings. (4) Conclusions: This pilot study establishes the feasibility of using unbiased quantitative phosphoproteomics to identify molecular perturbations associated with disease progression in Barrett's esophagus to define potentially clinically actionable targets warranting further assessment.

Published
2022

9. Receptor binding specificity of recent human H3N2 influenza viruses

Author

Cummings Richard D, Gulati Upma, Smith David F, Gulati Shelly, Kumari Kshama, and Air Gillian M

Subjects
Infectious and parasitic diseases, RC109-216
Abstract

Abstract Background Human influenza viruses are known to bind to sialic acid linked α2-6 to galactose, but the binding specificity beyond that linkage has not been systematically examined. H3N2 human influenza isolates lost binding to chicken red cells in the 1990s but viruses isolated since 2003 have re-acquired the ability to agglutinate chicken erythrocytes. We have investigated specificity of binding, changes in hemagglutinin sequence of the recent viruses and the role of sialic acid in productive infection. Results Viruses that agglutinate, or do not agglutinate, chicken red cells show identical binding to a Glycan Array of 264 oligosaccharides, binding exclusively to a subset of α2-6-sialylsaccharides. We identified an amino acid change in hemagglutinin that seemed to correlate with chicken red cell binding but when tested by mutagenesis there was no effect. Recombinant hemagglutinins expressed on Sf-9 cells bound chicken red cells but the released recombinant baculoviruses agglutinated only human red cells. Similarly, an isolate that does not agglutinate chicken red cells show hemadsorption of chicken red cells to infected MDCK cells. We suggest that binding of chicken red cells to cell surface hemagglutinin but not to virions is due to a more favorable hemagglutinin density on the cell surface. We investigated whether a virus specific for α2-6 sialyloligosaccharides shows differential entry into cells that have varying proportions of α2-6 and α2-3 sialic acids, including human A549 and HeLa cells with high levels of α2-6 sialic acid, and CHO cells that have only α2-3 sialic acid. We found that the virus enters all cell types tested and synthesizes viral nucleoprotein, localized in the nucleus, and hemagglutinin, transported to the cell surface, but infectious progeny viruses were released only from MDCK cells. Conclusion Agglutination of chicken red cells does not correlate with altered binding to any oligosaccharide on the Glycan Array, and may result from increased avidity due to density of hemagglutinin and not increased affinity. Absence of α2-6 sialic acid does not protect a cell from influenza infection and the presence of high levels of α2-6-sialic acids on a cell surface does not guarantee productive replication of a virus with α2-6 receptor specificity.

Published
2007
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10. Neuroprotective Effect of Exogenous Galectin-1 in Status Epilepticus

Author

Pacheco, Amanda Larissa Dias, de Melo, Igor Santana, de Araujo Costa, Maisa, Amaral, Mariah Morais Celestino, de Gusmão Taveiros Silva, Nívea Karla, Santos, Yngrid Mickaelli Oliveira, Gitaí, Daniel Leite Góes, Duzzioni, Marcelo, Borbely, Alexandre Urban, Silva, Robinson Sabino, Donatti, Ana Luiza Ferreira, Mestriner, Luisa, Fuzo, Carlos Alessandro, Cummings, Richard D., Garcia-Cairasco, Norberto, Dias-Baruffi, Marcelo, and de Castro, Olagide Wagner

Published
2022
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34. Parallel Glyco-SPOT Synthesis of Glycopeptide Libraries

Author

Mehta, Akul Y., Veeraiah, Ravi Kumar H., Dutta, Sucharita, Goth, Christoffer K., Hanes, Melinda S., Gao, Chao, Stavenhagen, Kathrin, Kardish, Robert, Matsumoto, Yasuyuki, Heimburg-Molinaro, Jamie, Boyce, Michael, Pohl, Nicola L.B., and Cummings, Richard D.

Published
2020
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43. Symbol Nomenclature for Graphical Representations of Glycans.

Author

Varki, Ajit, Cummings, Richard D, Aebi, Markus, Packer, Nicole H, Seeberger, Peter H, Esko, Jeffrey D, Stanley, Pamela, Hart, Gerald, Darvill, Alan, Kinoshita, Taroh, Prestegard, James J, Schnaar, Ronald L, Freeze, Hudson H, Marth, Jamey D, Bertozzi, Carolyn R, Etzler, Marilynn E, Frank, Martin, Vliegenthart, Johannes Fg, Lütteke, Thomas, Perez, Serge, Bolton, Evan, Rudd, Pauline, Paulson, James, Kanehisa, Minoru, Toukach, Philip, Aoki-Kinoshita, Kiyoko F, Dell, Anne, Narimatsu, Hisashi, York, William, Taniguchi, Naoyuki, and Kornfeld, Stuart

Subjects
Animals, Polysaccharides, Carbohydrate Conformation, Publishing, Terminology as Topic, Databases, Chemical, Biological Sciences, Medical and Health Sciences, Biochemistry & Molecular Biology
Published
2015

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