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Chuzel L, Fossa SL, Boisvert ML, et al. Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans. Microb Cell Fact. 2021;20(1):162doi: 10.1186/s12934-021-01652-w.
Chuzel, L., Fossa, S. L., Boisvert, M. L., Cajic, S., Hennig, R., Ganatra, M. B., Reichl, U., Rapp, E., & Taron, C. H. (2021). Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans. Microbial cell factories, 20(1), 162. https://doi.org/10.1186/s12934-021-01652-w
Chuzel, Léa, et al. "Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans." Microbial cell factories vol. 20,1 (2021): 162. doi: https://doi.org/10.1186/s12934-021-01652-w
Chuzel L, Fossa SL, Boisvert ML, Cajic S, Hennig R, Ganatra MB, Reichl U, Rapp E, Taron CH. Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans. Microb Cell Fact. 2021 Aug 21;20(1):162. doi: 10.1186/s12934-021-01652-w. PMID: 34419057; PMCID: PMC8379841.
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Microb Cell Fact. 2021 Aug 21;20(1):162. doi: 10.1186/s12934-021-01652-w.

Combining functional metagenomics and glycoanalytics to identify enzymes that facilitate structural characterization of sulfated N-glycans.

Microbial cell factories

Léa Chuzel, Samantha L Fossa, Madison L Boisvert, Samanta Cajic, René Hennig, Mehul B Ganatra, Udo Reichl, Erdmann Rapp, Christopher H Taron

Affiliations

  1. Bioprocess Engineering, Max Planck Institute for Dynamics of Complex Technical Systems, 39106, Magdeburg, Germany.
  2. New England Biolabs, Ipswich, MA, 01938, USA.
  3. glyXera GmbH, 39120, Magdeburg, Germany.
  4. Chair of Bioprocess Engineering, Otto-von-Guericke University, 39106, Magdeburg, Germany.
  5. New England Biolabs, Ipswich, MA, 01938, USA. [email protected].

PMID: 34419057 PMCID: PMC8379841 DOI: 10.1186/s12934-021-01652-w

Abstract

BACKGROUND: Sulfate modification of N-glycans is important for several biological functions such as clearance of pituitary hormones or immunoregulation. Yet, the prevalence of this N-glycan modification and its functions remain largely unexplored. Characterization of N-glycans bearing sulfate modifications is hampered in part by a lack of enzymes that enable site-specific detection of N-glycan sulfation. In this study, we used functional metagenomic screening to identify enzymes that act upon sulfated N-acetylglucosamine (GlcNAc). Using multiplexed capillary gel electrophoresis with laser-induced fluorescence detection (xCGE-LIF) -based glycoanalysis we proved their ability to act upon GlcNAc-6-SO

RESULTS: Our screen identified a sugar-specific sulfatase that specifically removes sulfate from GlcNAc-6-SO

CONCLUSION: The present study demonstrates the feasibility of using functional metagenomic screening combined with glycoanalytics to discover enzymes that act upon chemical modifications of glycans. The discovered enzymes represent new specificities that can help resolve the presence of GlcNAc-6-SO

© 2021. The Author(s).

Keywords: Functional metagenomics; Glycan analysis; Glycan sulfation; Glycoanalytics; Human microbiome; N-acetylglucosamine-6-sulfate; Sulfatase

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