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Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors

van Sorge, Nina M. ; Bonsor, Daniel A. ; Deng, Liwen ; Lindahl, Erik ; Schmitt, Verena ; Lyndin, Mykola ; Schmidt, Alexej ; Nilsson, Olof R. ; Brizuela, Jaime and Boero, Elena , et al. (2021) In EMBO Journal 40(7).
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 surface-expressed β protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in β 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... (More)

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 surface-expressed β protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in β 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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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Adhesin, IgI, immunoglobulin superfamily, receptor, Streptococcus agalactiae
in
EMBO Journal
volume
40
issue
7
publisher
Oxford University Press
external identifiers
  • scopus:85100313220
  • pmid:33522633
ISSN
0261-4189
DOI
10.15252/embj.2020106103
language
English
LU publication?
yes
id
9077d226-d0c3-41eb-b577-efd9a5ab43f8
date added to LUP
2021-02-12 13:26:00
date last changed
2024-06-13 07:01:45
@article{9077d226-d0c3-41eb-b577-efd9a5ab43f8,
  abstract     = {{<p>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 surface-expressed β protein of GBS binds to human CEACAM1 and CEACAM5 receptors. A crystal structure of the complex showed that an IgSF domain in β 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.</p>}},
  author       = {{van Sorge, Nina M. and Bonsor, Daniel A. and Deng, Liwen and Lindahl, Erik and Schmitt, Verena and Lyndin, Mykola and Schmidt, Alexej and Nilsson, Olof R. and Brizuela, Jaime and Boero, Elena and Sundberg, Eric J. and van Strijp, Jos A.G. and Doran, Kelly S. and Singer, Bernhard B. and Lindahl, Gunnar and McCarthy, Alex J.}},
  issn         = {{0261-4189}},
  keywords     = {{Adhesin; IgI; immunoglobulin superfamily; receptor; Streptococcus agalactiae}},
  language     = {{eng}},
  month        = {{02}},
  number       = {{7}},
  publisher    = {{Oxford University Press}},
  series       = {{EMBO Journal}},
  title        = {{Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors}},
  url          = {{http://dx.doi.org/10.15252/embj.2020106103}},
  doi          = {{10.15252/embj.2020106103}},
  volume       = {{40}},
  year         = {{2021}},
}