Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.
Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia, which has two distinct domains with unique specificities and biologi...
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2011
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oai:doaj.org-article:76f914195eee4f76922606de2f2949c02021-11-18T06:03:00ZBurkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity.1553-73661553-737410.1371/journal.ppat.1002238https://doaj.org/article/76f914195eee4f76922606de2f2949c02011-09-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21909279/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia, which has two distinct domains with unique specificities and biological activities. The N-terminal domain is a novel TNF-α-like fucose-binding lectin, while the C-terminal part is similar to a superfamily of calcium-dependent bacterial lectins. The C-terminal domain displays specificity for mannose and l-glycero-d-manno-heptose. BC2L-C is therefore a superlectin that binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes. The apo form of the C-terminal domain crystallized as a dimer, and calcium and mannose could be docked in the binding site. The whole lectin is hexameric and the overall structure, determined by electron microscopy and small angle X-ray scattering, reveals a flexible arrangement of three mannose/heptose-specific dimers flanked by two fucose-specific TNF-α-like trimers. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-α-like domain triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, and is therefore proposed to play a role in the dysregulated proinflammatory response observed in B. cenocepacia lung infections. The unique architecture of this newly recognized superlectin correlates with multiple functions including bacterial cell cross-linking, adhesion to human epithelia, and stimulation of inflammation.Ondřej SulákGianluca CiociEmilie LameignèreViviane BalloyAdam RoundIrina GutscheLenka MalinovskáMichel ChignardPaul KosmaDaniel F AubertCristina L MaroldaMiguel A ValvanoMichaela WimmerováAnne ImbertyPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 7, Iss 9, p e1002238 (2011) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 |
| spellingShingle |
Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Ondřej Sulák Gianluca Cioci Emilie Lameignère Viviane Balloy Adam Round Irina Gutsche Lenka Malinovská Michel Chignard Paul Kosma Daniel F Aubert Cristina L Marolda Miguel A Valvano Michaela Wimmerová Anne Imberty Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| description |
Lectins and adhesins are involved in bacterial adhesion to host tissues and mucus during early steps of infection. We report the characterization of BC2L-C, a soluble lectin from the opportunistic pathogen Burkholderia cenocepacia, which has two distinct domains with unique specificities and biological activities. The N-terminal domain is a novel TNF-α-like fucose-binding lectin, while the C-terminal part is similar to a superfamily of calcium-dependent bacterial lectins. The C-terminal domain displays specificity for mannose and l-glycero-d-manno-heptose. BC2L-C is therefore a superlectin that binds independently to mannose/heptose glycoconjugates and fucosylated human histo-blood group epitopes. The apo form of the C-terminal domain crystallized as a dimer, and calcium and mannose could be docked in the binding site. The whole lectin is hexameric and the overall structure, determined by electron microscopy and small angle X-ray scattering, reveals a flexible arrangement of three mannose/heptose-specific dimers flanked by two fucose-specific TNF-α-like trimers. We propose that BC2L-C binds to the bacterial surface in a mannose/heptose-dependent manner via the C-terminal domain. The TNF-α-like domain triggers IL-8 production in cultured airway epithelial cells in a carbohydrate-independent manner, and is therefore proposed to play a role in the dysregulated proinflammatory response observed in B. cenocepacia lung infections. The unique architecture of this newly recognized superlectin correlates with multiple functions including bacterial cell cross-linking, adhesion to human epithelia, and stimulation of inflammation. |
| format |
article |
| author |
Ondřej Sulák Gianluca Cioci Emilie Lameignère Viviane Balloy Adam Round Irina Gutsche Lenka Malinovská Michel Chignard Paul Kosma Daniel F Aubert Cristina L Marolda Miguel A Valvano Michaela Wimmerová Anne Imberty |
| author_facet |
Ondřej Sulák Gianluca Cioci Emilie Lameignère Viviane Balloy Adam Round Irina Gutsche Lenka Malinovská Michel Chignard Paul Kosma Daniel F Aubert Cristina L Marolda Miguel A Valvano Michaela Wimmerová Anne Imberty |
| author_sort |
Ondřej Sulák |
| title |
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| title_short |
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| title_full |
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| title_fullStr |
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| title_full_unstemmed |
Burkholderia cenocepacia BC2L-C is a super lectin with dual specificity and proinflammatory activity. |
| title_sort |
burkholderia cenocepacia bc2l-c is a super lectin with dual specificity and proinflammatory activity. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2011 |
| url |
https://doaj.org/article/76f914195eee4f76922606de2f2949c0 |
| work_keys_str_mv |
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