Sökning: onr:"swepub:oai:lup.lub.lu.se:4665c841-857f-4dd8-a5d4-50c0e7501fdf" > Human CEACAM1 is ta...
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000 | 03890naa a2200409 4500 | |
001 | oai:lup.lub.lu.se:4665c841-857f-4dd8-a5d4-50c0e7501fdf | |
003 | SwePub | |
008 | 230607s2023 | |||||||||||000 ||eng| | |
024 | 7 | a https://lup.lub.lu.se/record/4665c841-857f-4dd8-a5d4-50c0e7501fdf2 URI |
024 | 7 | a https://doi.org/10.1038/s41467-023-37732-12 DOI |
040 | a (SwePub)lu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a art2 swepub-publicationtype |
072 | 7 | a ref2 swepub-contenttype |
100 | 1 | a Catton, Erin A.u Imperial College London4 aut |
245 | 1 0 | a Human CEACAM1 is targeted by a Streptococcus pyogenes adhesin implicated in puerperal sepsis pathogenesis |
264 | 1 | c 2023 |
520 | a Life-threatening bacterial infections in women after childbirth, known as puerperal sepsis, resulted in classical epidemics and remain a global health problem. While outbreaks of puerperal sepsis have been ascribed to Streptococcus pyogenes, little is known about disease mechanisms. Here, we show that the bacterial R28 protein, which is epidemiologically associated with outbreaks of puerperal sepsis, specifically targets the human receptor CEACAM1. This interaction triggers events that would favor the development of puerperal sepsis, including adhesion to cervical cells, suppression of epithelial wound repair and subversion of innate immune responses. High-resolution structural analysis showed that an R28 domain with IgI3-like fold binds to the N-terminal domain of CEACAM1. Together, these findings demonstrate that a single adhesin-receptor interaction can drive the pathogenesis of bacterial sepsis and provide molecular insights into the pathogenesis of one of the most important infectious diseases in medical history. | |
650 | 7 | a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Mikrobiologi inom det medicinska området0 (SwePub)301092 hsv//swe |
650 | 7 | a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Microbiology in the medical area0 (SwePub)301092 hsv//eng |
700 | 1 | a Bonsor, Daniel A.u University of Maryland, Baltimore4 aut |
700 | 1 | a Herrera, Carolinau Imperial College London4 aut |
700 | 1 | a Stålhammar-Carlemalm, Margarethau Lund University,Lunds universitet,Avdelningen för medicinsk mikrobiologi,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Medical Microbiology,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)mmb-msc |
700 | 1 | a Lyndin, Mykolau Sumy State University,University Hospital Essen4 aut |
700 | 1 | a Turner, Claire E.u University of Sheffield4 aut |
700 | 1 | a Soden, Jo4 aut |
700 | 1 | a van Strijp, Jos A.G.u University Medical Center Utrecht4 aut |
700 | 1 | a Singer, Bernhard B.u University of Duisburg-Essen4 aut |
700 | 1 | a van Sorge, Nina M.u University Medical Center Utrecht,Academic Medical Center of University of Amsterdam (AMC)4 aut |
700 | 1 | a Lindahl, Gunnaru 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, LTH4 aut0 (Swepub:lu)mmb-gli |
700 | 1 | a McCarthy, Alex J.u University Medical Center Utrecht,Imperial College London4 aut |
710 | 2 | a Imperial College Londonb University of Maryland, Baltimore4 org |
773 | 0 | t Nature Communicationsg 14q 14x 2041-1723 |
856 | 4 | u http://dx.doi.org/10.1038/s41467-023-37732-1x freey FULLTEXT |
856 | 4 8 | u https://lup.lub.lu.se/record/4665c841-857f-4dd8-a5d4-50c0e7501fdf |
856 | 4 8 | u https://doi.org/10.1038/s41467-023-37732-1 |
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