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Bacterial protein d...
Bacterial protein domains with a novel Ig-like fold target human CEACAM receptors
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- van Sorge, Nina M. (author)
- Department of Medical Microbiology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands; Department of Medical Microbiology, Infection Prevention and Netherlands Reference Laboratory for Bacterial Meningitis, Amsterdam University Medical Center, University of Amsterdam, Amsterdam, Netherlands
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- Bonsor, Daniel A. (author)
- Institute of Human Virology, University of Maryland School of Medicine, University of Maryland, MD, Baltimore, United States
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- Deng, Liwen (author)
- Department of Immunology & Microbiology, University of Colorado Anschutz Medical Campus, CO, Aurora, United States
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- Lindahl, Erik (author)
- Stockholm University
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- Schmitt, Verena (author)
- Institute of Anatomy, Medical Faculty, University Duisburg-Essen, Essen, Germany
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- Lyndin, Mykola (author)
- Institute of Anatomy, Medical Faculty, University Duisburg-Essen, Essen, Germany; Department of Pathology, Sumy State University, Sumy, Ukraine
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- Schmidt, Alexej (author)
- Umeå University,Umeå universitet,Patologi
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- Nilsson, Olof R. (author)
- Department of Laboratory Medicine, Division of Medical Microbiology, Lund University, Lund, Sweden
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- Brizuela, Jaime (author)
- Department of Infectious Disease, MRC Centre for Molecular Bacteriology & Infection, Imperial College London, London, United Kingdom
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- Boero, Elena (author)
- Department of Medical Microbiology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands
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- Sundberg, Eric J. (author)
- Institute of Human Virology, University of Maryland School of Medicine, University of Maryland, MD, Baltimore, United States; Department of Biochemistry, Emory University School of Medicine, GA, Atlanta, United States
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- van Strijp, Jos A. G. (author)
- Department of Medical Microbiology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands
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- Doran, Kelly S. (author)
- Department of Immunology & Microbiology, University of Colorado Anschutz Medical Campus, CO, Aurora, United States
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- Singer, Bernhard B. (author)
- Institute of Anatomy, Medical Faculty, University Duisburg-Essen, Essen, Germany
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- Lindahl, Gunnar (author)
- Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Teknisk mikrobiologi,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine,Applied Microbiology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH
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- McCarthy, Alex J. (author)
- Department of Medical Microbiology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands; Department of Infectious Disease, MRC Centre for Molecular Bacteriology & Infection, Imperial College London, London, United Kingdom
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(creator_code:org_t)
- 2021-02
- 2021
- English.
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In: EMBO Journal. - : Wiley-VCH Verlagsgesellschaft. - 0261-4189 .- 1460-2075. ; 40
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Abstract
Subject headings
Close
- 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.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- Adhesin
- IgI
- immunoglobulin superfamily
- receptor
- Streptococcus agalactiae
- Adhesin
- IgI
- immunoglobulin superfamily
- receptor
- Streptococcus agalactiae
Publication and Content Type
- ref (subject category)
- art (subject category)
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To the university's database
- By the author/editor
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van Sorge, Nina ...
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Bonsor, Daniel A ...
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Deng, Liwen
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Lindahl, Erik
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Schmitt, Verena
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Lyndin, Mykola
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show more...
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Schmidt, Alexej
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Nilsson, Olof R.
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Brizuela, Jaime
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Boero, Elena
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Sundberg, Eric J ...
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van Strijp, Jos ...
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Doran, Kelly S.
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Singer, Bernhard ...
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Lindahl, Gunnar
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McCarthy, Alex J ...
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- About the subject
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- MEDICAL AND HEALTH SCIENCES
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MEDICAL AND HEAL ...
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and Basic Medicine
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and Microbiology in ...
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- NATURAL SCIENCES
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
- Articles in the publication
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EMBO Journal
- By the university
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Umeå University
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Lund University