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A single sulfatase is required to access colonic mucin by a gut bacterium.
Luis, Ana S; Jin, Chunsheng; Pereira, Gabriel Vasconcelos; Glowacki, Robert W P; Gugel, Sadie R; Singh, Shaleni; Byrne, Dominic P; Pudlo, Nicholas A; London, James A; Baslé, Arnaud; Reihill, Mark; Oscarson, Stefan; Eyers, Patrick A; Czjzek, Mirjam; Michel, Gurvan; Barbeyron, Tristan; Yates, Edwin A; Hansson, Gunnar C; Karlsson, Niclas G; Cartmell, Alan; Martens, Eric C.
Afiliación
  • Luis AS; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA. ana.luis@medkem.gu.se.
  • Jin C; Department of Medical Biochemistry, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden. ana.luis@medkem.gu.se.
  • Pereira GV; Department of Medical Biochemistry, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Glowacki RWP; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
  • Gugel SR; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
  • Singh S; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
  • Byrne DP; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
  • Pudlo NA; Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
  • London JA; Department of Microbiology and Immunology, University of Michigan, Ann Arbor, MI, USA.
  • Baslé A; Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
  • Reihill M; Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK.
  • Oscarson S; Centre for Synthesis and Chemical Biology, University College Dublin, Belfield, Dublin, Ireland.
  • Eyers PA; Centre for Synthesis and Chemical Biology, University College Dublin, Belfield, Dublin, Ireland.
  • Czjzek M; Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
  • Michel G; Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Roscoff, Bretagne, France.
  • Barbeyron T; Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Roscoff, Bretagne, France.
  • Yates EA; Sorbonne Université, Univ Paris 06, CNRS, UMR 8227, Integrative Biology of Marine Models, Roscoff, Bretagne, France.
  • Hansson GC; Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK.
  • Karlsson NG; Department of Medical Biochemistry, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Cartmell A; Department of Medical Biochemistry, Institute for Biomedicine, Sahlgrenska Academy, University of Gothenburg, Gothenburg, Sweden.
  • Martens EC; Department of Biochemistry and Systems Biology, Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, UK. alan.cartmell@liverpool.ac.uk.
Nature ; 598(7880): 332-337, 2021 10.
Article en En | MEDLINE | ID: mdl-34616040
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfatasas / Bacteroides / Colon / Microbioma Gastrointestinal / Mucinas Límite: Animals / Female / Humans / Male Idioma: En Revista: Nature Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Sulfatasas / Bacteroides / Colon / Microbioma Gastrointestinal / Mucinas Límite: Animals / Female / Humans / Male Idioma: En Revista: Nature Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido