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Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori

Research output: Contribution to journal › Article › peer-review

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Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori. / Moonens, K.; Gideonsson, P.; Subedi, S. et al.
In: Cell Host and Microbe, Vol. 19, No. 1, 13.01.2016, p. 55-66.

Research output: Contribution to journal › Article › peer-review

HarvardHarvard

Moonens, K, Gideonsson, P, Subedi, S, Bugaytsova, J, Romaõ, E, Mendez, M, Nordén, J, Fallah, M, Rakhimova, L, Shevtsova, A, Lahmann, M, Castaldo, G, Brännström, K, Coppens, F, Lo, AW, Ny, T, Solnick, JV, Vandenbussche, G, Oscarson, S, Hammarström, L, Arnqvist, A, Berg, DE, Muyldermans, S, Borén, T & Remaut, H 2016, 'Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori', Cell Host and Microbe, vol. 19, no. 1, pp. 55-66. https://doi.org/10.1016/j.chom.2015.12.004

APA

Moonens, K., Gideonsson, P., Subedi, S., Bugaytsova, J., Romaõ, E., Mendez, M., Nordén, J., Fallah, M., Rakhimova, L., Shevtsova, A., Lahmann, M., Castaldo, G., Brännström, K., Coppens, F., Lo, A. W., Ny, T., Solnick, J. V., Vandenbussche, G., Oscarson, S., ... Remaut, H. (2016). Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori. Cell Host and Microbe, 19(1), 55-66. https://doi.org/10.1016/j.chom.2015.12.004

CBE

Moonens K, Gideonsson P, Subedi S, Bugaytsova J, Romaõ E, Mendez M, Nordén J, Fallah M, Rakhimova L, Shevtsova A, et al. 2016. Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori. Cell Host and Microbe. 19(1):55-66. https://doi.org/10.1016/j.chom.2015.12.004

MLA

Moonens, K. et al. "Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori". Cell Host and Microbe. 2016, 19(1). 55-66. https://doi.org/10.1016/j.chom.2015.12.004

VancouverVancouver

Moonens K, Gideonsson P, Subedi S, Bugaytsova J, Romaõ E, Mendez M et al. Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori. Cell Host and Microbe. 2016 Jan 13;19(1):55-66. doi: 10.1016/j.chom.2015.12.004

Author

Moonens, K. ; Gideonsson, P. ; Subedi, S. et al. / Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori. In: Cell Host and Microbe. 2016 ; Vol. 19, No. 1. pp. 55-66.

RIS

TY - JOUR

T1 - Structural Insights into Polymorphic ABO Glycan Binding by Helicobacter pylori

AU - Moonens, K.

AU - Gideonsson, P.

AU - Subedi, S.

AU - Bugaytsova, J.

AU - Romaõ, E.

AU - Mendez, M.

AU - Nordén, J.

AU - Fallah, M.

AU - Rakhimova, L.

AU - Shevtsova, A.

AU - Lahmann, Martina

AU - Castaldo, G.

AU - Brännström, K.

AU - Coppens, F.

AU - Lo, A.W.

AU - Ny, T.

AU - Solnick, J.V.

AU - Vandenbussche, G.

AU - Oscarson, S.

AU - Hammarström, L.

AU - Arnqvist, A.

AU - Berg, D.E.

AU - Muyldermans, S.

AU - Borén, T.

AU - Remaut, H.

PY - 2016/1/13

Y1 - 2016/1/13

N2 - The Helicobacter pylori adhesin BabA binds mucosal ABO/Leb blood group (bg) carbohydrates. BabA facilitates bacterial attachment to gastric surfaces, increasing strain virulence and forming a recognized risk factor for peptic ulcers and gastric cancer. High sequence variation causes BabA functional diversity, but the underlying structural-molecular determinants are unknown. We generated X-ray structures of representative BabA isoforms that reveal a polymorphic, three-pronged Leb binding site. Two diversity loops, DL1 and DL2, provide adaptive control to binding affinity, notably ABO versus O bg preference. H. pylori strains can switch bg preference with single DL1 amino acid substitutions, and can coexpress functionally divergent BabA isoforms. The anchor point for receptor binding is the embrace of an ABO fucose residue by a disulfide-clasped loop, which is inactivated by reduction. Treatment with the redoxactive pharmaceutic N-acetylcysteine lowers gastric mucosal neutrophil infiltration in H. pylori-infected Leb-expressing mice, providing perspectives on possible H. pylori eradication therapies.

AB - The Helicobacter pylori adhesin BabA binds mucosal ABO/Leb blood group (bg) carbohydrates. BabA facilitates bacterial attachment to gastric surfaces, increasing strain virulence and forming a recognized risk factor for peptic ulcers and gastric cancer. High sequence variation causes BabA functional diversity, but the underlying structural-molecular determinants are unknown. We generated X-ray structures of representative BabA isoforms that reveal a polymorphic, three-pronged Leb binding site. Two diversity loops, DL1 and DL2, provide adaptive control to binding affinity, notably ABO versus O bg preference. H. pylori strains can switch bg preference with single DL1 amino acid substitutions, and can coexpress functionally divergent BabA isoforms. The anchor point for receptor binding is the embrace of an ABO fucose residue by a disulfide-clasped loop, which is inactivated by reduction. Treatment with the redoxactive pharmaceutic N-acetylcysteine lowers gastric mucosal neutrophil infiltration in H. pylori-infected Leb-expressing mice, providing perspectives on possible H. pylori eradication therapies.

U2 - 10.1016/j.chom.2015.12.004

DO - 10.1016/j.chom.2015.12.004

M3 - Article

VL - 19

SP - 55

EP - 66

JO - Cell Host and Microbe

JF - Cell Host and Microbe

SN - 1931-3128

IS - 1

ER -