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Title | Bacterial protein domains with a novel Ig-like foldtarget human CEAC AM receptors |
Authors |
Sorge, N.M.
Bonsor, D.A. Deng, L. Lindahl, E. Schmitt, V. Lyndin, Mykola Serhiiovych Schmidt, A. Nilsson, O.R. Brizuela, J. Boero, E. Sundberg, E.J. Strijp, J.A.G. Doran, K.S. Singer, B.B. Lindahl, G. McCarth, A.J. |
ORCID |
http://orcid.org/0000-0003-4385-3903 |
Keywords |
Adhesin immunoglobulin superfamily IgI receptor Streptococcus agalactiae |
Type | Article |
Date of Issue | 2021 |
URI | https://essuir.sumdu.edu.ua/handle/123456789/83279 |
Publisher | John Wiley and Sons |
License | Creative Commons Attribution 4.0 International License |
Citation | Sorge NM, Bonsor DA, Deng L, Lindahl E, Schmitt V, Lyndin MS, Schmidt A, Nilsson OR, Brizuela J, Boero E, Sundberg EJ, Strijp JAG, Doran KS, Singer BB, Lindahl G, McCarth A.J (2021) Bacterial protein domains with a novel Ig‐like fold target human CEACAM receptors The EMBO Journal 40: e106103. https://doi.org/10.15252/embj.2020106103 |
Abstract |
Streptococcus agalactiae, also known as group B Streptococcus (GBS), is the major cause of neonatal sepsis in humans. A critical step to infection is adhesion of bacteria to epithelial surfaces. GBS adhesins
have been identified to bind extracellular matrix components and cellular receptors. However, several putative adhesins have no host binding partner characterised. We report here that surfaceexpressed b protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF
domain in b represents a novel Ig-fold subtype called IgI3, in which unique features allow binding to CEACAM1. Bioinformatic assessment revealed that this newly identified IgI3 fold is not exclusively present in GBS but is predicted to be present in adhesins from other clinically important human pathogens. In agreement with this
prediction, we found that CEACAM1 binds to an IgI3 domain found in an adhesin from a different streptococcal species. Overall, our results indicate that the IgI3 fold could provide a broadly applied
mechanism for bacteria to target CEACAMs. |
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File | Size | Format | Downloads |
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Sorge_et.al._Bacterial_protein_2021.pdf | 2.77 MB | Adobe PDF | 44318957 |
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