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DOI10.1073/PNAS.2014444118
Staphylococcus aureus binds to the N-terminal region of corneodesmosin to adhere to the stratum corneum in atopic dermatitis
Towell A.M.; Feuillie C.; Vitry P.; da Costa T.M.; Mathelié-Guinlet M.; Kezic S.; Fleury O.M.; McAleer M.A.; Dufrêne Y.F.; Irvine A.D.; Geoghegan J.A.
发表日期2021
ISSN00278424
卷号118期号:1
英文摘要Staphylococcus aureus colonizes the skin of the majority of patients with atopic dermatitis (AD), and its presence increases disease severity. Adhesion of S. aureus to corneocytes in the stratum corneum is a key initial event in colonization, but the bacterial and host factors contributing to this process have not been defined. Here, we show that S. aureus interacts with the host protein corneodesmosin. Corneodesmosin is aberrantly displayed on the tips of villus-like projections that occur on the surface of AD corneocytes as a result of low levels of skin humectants known as natural moisturizing factor (NMF). An S. aureus mutant deficient in fibronectin binding protein B (FnBPB) and clumping factor B (ClfB) did not bind to corneodesmosin in vitro. Using surface plasmon resonance, we found that FnBPB and ClfB proteins bound with similar affinities. The S. aureus binding site was localized to the N-terminal glycine–serine-rich region of corneodesmosin. Atomic force microscopy showed that the N-terminal region was present on corneocytes containing low levels of NMF and that blocking it with an antibody inhibited binding of individual S. aureus cells to corneocytes. Finally, we found that S. aureus mutants deficient in FnBPB or ClfB have a reduced ability to adhere to low-NMF corneocytes from patients. In summary, we show that FnBPB and ClfB interact with the accessible N-terminal region of corneodesmosin on AD corneocytes, allowing S. aureus to take advantage of the aberrant display of corneodesmosin that accompanies low NMF in AD. This interaction facilitates the characteristic strong binding of S. aureus to AD corneocytes. © 2021 National Academy of Sciences. All rights reserved.
英文关键词Adhesion; Bacteria; Colonization; Corneocytes; Staphylococcus aureus
语种英语
scopus关键词cell protein; corneodesmosin; fibronectin binding protein; unclassified drug; amino terminal sequence; Article; atomic force microscopy; atopic dermatitis; bacterial cell; binding affinity; binding site; controlled study; host interaction; human; human tissue; microbial interaction; nonhuman; priority journal; protein localization; Staphylococcus aureus; stratum corneum; surface plasmon resonance
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/181132
作者单位Department of Microbiology, Moyne Institute of Preventive Medicine, School of Genetics and Microbiology, Trinity College Dublin, Dublin 2, Ireland; Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, B-1348, Belgium; Coronel Institute of Occupational Health, Amsterdam Public Health Research Institute, University Medical Center, University of Amsterdam, Amsterdam, 1105 AZ, Netherlands; Clinical Medicine, Trinity College Dublin, Dublin 2, Ireland; Walloon Excellence in Life Sciences and Biotechnology, Wavre, B-1300, Belgium; Institute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Birmingham, B15 2TT, United Kingdom
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Towell A.M.,Feuillie C.,Vitry P.,et al. Staphylococcus aureus binds to the N-terminal region of corneodesmosin to adhere to the stratum corneum in atopic dermatitis[J],2021,118(1).
APA Towell A.M..,Feuillie C..,Vitry P..,da Costa T.M..,Mathelié-Guinlet M..,...&Geoghegan J.A..(2021).Staphylococcus aureus binds to the N-terminal region of corneodesmosin to adhere to the stratum corneum in atopic dermatitis.Proceedings of the National Academy of Sciences of the United States of America,118(1).
MLA Towell A.M.,et al."Staphylococcus aureus binds to the N-terminal region of corneodesmosin to adhere to the stratum corneum in atopic dermatitis".Proceedings of the National Academy of Sciences of the United States of America 118.1(2021).
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