A single sulfatase is required to access colonic mucin by a gut bacterium

Ana S. Luis (), Chunsheng Jin, Gabriel Vasconcelos Pereira, Robert W. P. Glowacki, Sadie R. Gugel, Shaleni Singh, Dominic P. Byrne, Nicholas A. Pudlo, James A. London, Arnaud Baslé, Mark Reihill, Stefan Oscarson, Patrick A. Eyers, Mirjam Czjzek, Gurvan Michel, Tristan Barbeyron, Edwin A. Yates, Gunnar C. Hansson, Niclas G. Karlsson, Alan Cartmell () and Eric C. Martens ()
Additional contact information
Ana S. Luis: University of Michigan
Chunsheng Jin: University of Gothenburg
Gabriel Vasconcelos Pereira: University of Michigan
Robert W. P. Glowacki: University of Michigan
Sadie R. Gugel: University of Michigan
Shaleni Singh: University of Michigan
Dominic P. Byrne: University of Liverpool
Nicholas A. Pudlo: University of Michigan
James A. London: University of Liverpool
Arnaud Baslé: Newcastle University
Mark Reihill: University College Dublin, Belfield
Stefan Oscarson: University College Dublin, Belfield
Patrick A. Eyers: University of Liverpool
Mirjam Czjzek: Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models
Gurvan Michel: Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models
Tristan Barbeyron: Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models
Edwin A. Yates: University of Liverpool
Gunnar C. Hansson: University of Gothenburg
Niclas G. Karlsson: University of Gothenburg
Alan Cartmell: University of Liverpool
Eric C. Martens: University of Michigan

Nature, 2021, vol. 598, issue 7880, 332-337

Abstract: Abstract Humans have co-evolved with a dense community of microbial symbionts that inhabit the lower intestine. In the colon, secreted mucus creates a barrier that separates these microorganisms from the intestinal epithelium1. Some gut bacteria are able to utilize mucin glycoproteins, the main mucus component, as a nutrient source. However, it remains unclear which bacterial enzymes initiate degradation of the complex O-glycans found in mucins. In the distal colon, these glycans are heavily sulfated, but specific sulfatases that are active on colonic mucins have not been identified. Here we show that sulfatases are essential to the utilization of distal colonic mucin O-glycans by the human gut symbiont Bacteroides thetaiotaomicron. We characterized the activity of 12 different sulfatases produced by this species, showing that they are collectively active on all known sulfate linkages in O-glycans. Crystal structures of three enzymes provide mechanistic insight into the molecular basis of substrate specificity. Unexpectedly, we found that a single sulfatase is essential for utilization of sulfated O-glycans in vitro and also has a major role in vivo. Our results provide insight into the mechanisms of mucin degradation by a prominent group of gut bacteria, an important process for both normal microbial gut colonization2 and diseases such as inflammatory bowel disease3.

Date: 2021
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/s41586-021-03967-5 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:598:y:2021:i:7880:d:10.1038_s41586-021-03967-5

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-021-03967-5

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().