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  Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. Hel_I_6 consumes alpha-mannan from fungi

Solanki, V., Krüger, K., Crawford, C., Pardo-Vargas, A., Danglad-Flores, J. A., Le Mai Hoang, K., et al. (2022). Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. Hel_I_6 consumes alpha-mannan from fungi. The ISME Journal, 16(7), 1818-1830. doi:10.1038/s41396-022-01223-w.

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Solanki, Vipul, Author
Krüger, Karen, Author
Crawford, Conor1, Author              
Pardo-Vargas, Alonso1, Author              
Danglad-Flores, José Angél1, Author              
Le Mai Hoang, Kim1, Author              
Klassen, Leeann, Author
Abbott, D. Wade, Author
Seeberger, Peter H.1, Author              
Amann, Rudolf I., Author
Teeling, Hanno, Author
Hehemann, Jan-Hendrik, Author
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1Peter H. Seeberger - Automated Systems, Biomolekulare Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863306              

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 Abstract: Microbial glycan degradation is essential to global carbon cycling. The marine bacterium Salegentibacter sp. Hel_I_6 (Bacteroidota) isolated from seawater off Helgoland island (North Sea) contains an α-mannan inducible gene cluster with a GH76 family endo-α-1,6-mannanase (ShGH76). This cluster is related to genetic loci employed by human gut bacteria to digest fungal α-mannan. Metagenomes from the Hel_I_6 isolation site revealed increasing GH76 gene frequencies in free-living bacteria during microalgae blooms, suggesting degradation of α-1,6-mannans from fungi. Recombinant ShGH76 protein activity assays with yeast α-mannan and synthetic oligomannans showed endo-α-1,6-mannanase activity. Resolved structures of apo-ShGH76 (2.0 Å) and of mutants co-crystalized with fungal mannan-mimicking α-1,6-mannotetrose (1.90 Å) and α-1,6-mannotriose (1.47 Å) retained the canonical (α/α)6 fold, despite low identities with sequences of known GH76 structures (GH76s from gut bacteria: <27%). The apo-form active site differed from those known from gut bacteria, and co-crystallizations revealed a kinked oligomannan conformation. Co-crystallizations also revealed precise molecular-scale interactions of ShGH76 with fungal mannan-mimicking oligomannans, indicating adaptation to this particular type of substrate. Our data hence suggest presence of yet unknown fungal α-1,6-mannans in marine ecosystems, in particular during microalgal blooms.

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Language(s): eng - English
 Dates: 2022-04-122022
 Publication Status: Published in print
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 Identifiers: DOI: 10.1038/s41396-022-01223-w
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Title: The ISME Journal
  Other : The ISME journal : multidisciplinary journal of microbial ecology
Source Genre: Journal
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Publ. Info: Basingstoke : Nature Publishing Group
Pages: - Volume / Issue: 16 (7) Sequence Number: - Start / End Page: 1818 - 1830 Identifier: ISSN: 1751-7370