Výsledky vyhledávání - "MESH: Staphylococcal Protein A"

The Role of Regulator Catabolite Control Protein A (CcpA) in Streptococcus agalactiae Physiology and Stress Response

Autor: Roux, Anne-Emmanuelle, Robert, Sylvie, Bastat, Mathilde, Rosinski-Chupin, Isabelle, Rong, Vanessa, Holbert, Sébastien, Mereghetti, Laurent, Camiade, Emilie

Publikováno v: Microbiology Spectrum
Microbiology Spectrum, 2022, 10 (6), pp.e02080-22. ⟨10.1128/spectrum.02080-22⟩

International audience; Abstract : Streptococcus agalactiae is a leading cause of infections in neonates. This opportunistic pathogen colonizes the vagina, where it has to cope with acidic pH and hydrogen peroxide produced by lactobacilli. Thus, in t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::48e34db333ea5626c3c2e6bb40264b62
https://pubmed.ncbi.nlm.nih.gov/36264242

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Exploration of the role of the virulence factor ElrA during Enterococcus faecalis cell infection

Autor: Stéphane Gaubert, Jean-Marie Herry, Romain Briandet, Julien Deschamps, Pascale Serror, Natalia Nunez, Yu Wei, Thomas Baranek, Mustapha Si-Tahar, Aurélie Derré-Bobillot, Cristel Archambaud

Publikováno v: Scientific Reports
Scientific Reports, Nature Publishing Group, 2018, 8 (1), ⟨10.1038/s41598-018-20206-6⟩
Scientific Reports, 2018, 8 (1), pp.1749. ⟨10.1038/s41598-018-20206-6⟩
Scientific Reports, Nature Publishing Group, 2018, 8 (1), pp.1749. ⟨10.1038/s41598-018-20206-6⟩
Scientific Reports 1749 (8), . (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-11 (2018)

Enterococcus faecalis, an organism generally not pathogenic for healthy humans, has the potential to cause disease in susceptible hosts. While it seems to be equipped to interact with and circumvent host immune defense, most of the molecular and cell

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::445d2457770e440b458cac9ff9824fbe
https://doi.org/10.1038/s41598-018-20206-6

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Prolonged display or rapid internalization of the IgG-binding protein ZZ anchored to the surface of cells using the diphtheria toxin T domain

Autor: Philippe Nizard, Daniel Gillet, Alain Fourcade, Alexandre Chenal, Bruno Beaumelle

Publikováno v: Protein Engineering, Design and Selection
Protein Engineering, Design and Selection, 2001, 14 (6), pp.439-446. ⟨10.1093/protein/14.6.439⟩
Protein Engineering, Design and Selection, Oxford University Press (OUP), 2001, 14 (6), pp.439-446. ⟨10.1093/protein/14.6.439⟩

International audience; We have shown previously that the diphtheria toxin transmembrane domain (T) may function as a membrane anchor for soluble proteins fused at its C-terminus. Binding to membranes is triggered by acidic pH. Here, we further chara

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15210f5efb739e1fe2f28ba66ec19ccc
https://pubmed.ncbi.nlm.nih.gov/11477224

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Increasing immunogenicity of antigens fused to Ig-binding proteins by cell surface targeting

Autor: Léonetti, M, Thai, Robert, Cotton, J, Leroy, S, Drevet, P, Ducancel, F, Boulain, J, Ménez, A

Publikováno v: Journal of Immunology
Journal of Immunology, 1998, 160 (8), pp.3820-7
Journal of Immunology, Publisher : Baltimore : Williams & Wilkins, c1950-. Latest Publisher : Bethesda, MD : American Association of Immunologists, 1998, 160 (8), pp.3820-7

Fusion of antigenic proteins to Ig-binding proteins such as protein A from Staphylococcus aureus and its derived ZZ fragment is known to increase immunogenicity of the fused Ag in vivo. To shed light on the origin of this effect, we used snake toxins

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::08f529447d78d1106f27f4a37a05d63a
https://hal.science/hal-03038950

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