Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation
Carbohydrate recognition by lectins governs critical host-microbe interactions. MpPA14 (Marinomonas primoryensis PA14 domain) lectin is a domain of a 1.5-MDa adhesin responsible for a symbiotic bacterium-diatom interaction in Antarctica. Here, we show that MpPA14 binds various monosaccharides, with...
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ftpubmed:oai:pubmedcentral.nih.gov:8092209 2023-05-15T13:54:07+02:00 Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation Guo, Shuaiqi Vance, Tyler D. R. Zahiri, Hossein Eves, Robert Stevens, Corey Hehemann, Jan-Hendrik Vidal-Melgosa, Silvia Davies, Peter L. 2021-04-06 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8092209/ http://www.ncbi.nlm.nih.gov/pubmed/33824212 https://doi.org/10.1128/mBio.00130-21 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8092209/ http://www.ncbi.nlm.nih.gov/pubmed/33824212 http://dx.doi.org/10.1128/mBio.00130-21 Copyright © 2021 Guo et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) . CC-BY mBio Research Article Text 2021 ftpubmed https://doi.org/10.1128/mBio.00130-21 2021-05-09T00:48:02Z Carbohydrate recognition by lectins governs critical host-microbe interactions. MpPA14 (Marinomonas primoryensis PA14 domain) lectin is a domain of a 1.5-MDa adhesin responsible for a symbiotic bacterium-diatom interaction in Antarctica. Here, we show that MpPA14 binds various monosaccharides, with l-fucose and N-acetylglucosamine being the strongest ligands (dissociation constant [K(d)], ∼150 μM). High-resolution structures of MpPA14 with 15 different sugars bound elucidated the molecular basis for the lectin’s apparent binding promiscuity but underlying selectivity. MpPA14 mediates strong Ca(2+)-dependent interactions with the 3,4-diols of l-fucopyranose and glucopyranoses, and it binds other sugars via their specific minor isomers. Thus, MpPA14 only binds polysaccharides like branched glucans and fucoidans with these free end groups. Consistent with our findings, adhesion of MpPA14 to diatom cells was selectively blocked by l-fucose, but not by N-acetyl galactosamine. The MpPA14 lectin homolog present in a Vibrio cholerae adhesin was produced and was shown to have the same sugar binding preferences as MpPA14. The pathogen’s lectin was unable to effectively bind the diatom in the presence of fucose, thus demonstrating the antiadhesion strategy of blocking infection via ligand-based antagonists. Text Antarc* Antarctica PubMed Central (PMC) mBio 12 2 |
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Research Article Guo, Shuaiqi Vance, Tyler D. R. Zahiri, Hossein Eves, Robert Stevens, Corey Hehemann, Jan-Hendrik Vidal-Melgosa, Silvia Davies, Peter L. Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
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Research Article |
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Carbohydrate recognition by lectins governs critical host-microbe interactions. MpPA14 (Marinomonas primoryensis PA14 domain) lectin is a domain of a 1.5-MDa adhesin responsible for a symbiotic bacterium-diatom interaction in Antarctica. Here, we show that MpPA14 binds various monosaccharides, with l-fucose and N-acetylglucosamine being the strongest ligands (dissociation constant [K(d)], ∼150 μM). High-resolution structures of MpPA14 with 15 different sugars bound elucidated the molecular basis for the lectin’s apparent binding promiscuity but underlying selectivity. MpPA14 mediates strong Ca(2+)-dependent interactions with the 3,4-diols of l-fucopyranose and glucopyranoses, and it binds other sugars via their specific minor isomers. Thus, MpPA14 only binds polysaccharides like branched glucans and fucoidans with these free end groups. Consistent with our findings, adhesion of MpPA14 to diatom cells was selectively blocked by l-fucose, but not by N-acetyl galactosamine. The MpPA14 lectin homolog present in a Vibrio cholerae adhesin was produced and was shown to have the same sugar binding preferences as MpPA14. The pathogen’s lectin was unable to effectively bind the diatom in the presence of fucose, thus demonstrating the antiadhesion strategy of blocking infection via ligand-based antagonists. |
format |
Text |
author |
Guo, Shuaiqi Vance, Tyler D. R. Zahiri, Hossein Eves, Robert Stevens, Corey Hehemann, Jan-Hendrik Vidal-Melgosa, Silvia Davies, Peter L. |
author_facet |
Guo, Shuaiqi Vance, Tyler D. R. Zahiri, Hossein Eves, Robert Stevens, Corey Hehemann, Jan-Hendrik Vidal-Melgosa, Silvia Davies, Peter L. |
author_sort |
Guo, Shuaiqi |
title |
Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
title_short |
Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
title_full |
Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
title_fullStr |
Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
title_full_unstemmed |
Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation |
title_sort |
structural basis of ligand selectivity by a bacterial adhesin lectin involved in multispecies biofilm formation |
publisher |
American Society for Microbiology |
publishDate |
2021 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8092209/ http://www.ncbi.nlm.nih.gov/pubmed/33824212 https://doi.org/10.1128/mBio.00130-21 |
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Antarc* Antarctica |
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Antarc* Antarctica |
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mBio |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8092209/ http://www.ncbi.nlm.nih.gov/pubmed/33824212 http://dx.doi.org/10.1128/mBio.00130-21 |
op_rights |
Copyright © 2021 Guo et al. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (https://creativecommons.org/licenses/by/4.0/) . |
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CC-BY |
op_doi |
https://doi.org/10.1128/mBio.00130-21 |
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mBio |
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