دورية أكاديمية

Transferrin-Binding Protein B Of Neisseria Meningitidis: Sequence-Based Identification Of The Transferrin-Binding Site Confirmed By Site-Directed Mutagenesis

التفاصيل البيبلوغرافية
العنوان: Transferrin-Binding Protein B Of Neisseria Meningitidis: Sequence-Based Identification Of The Transferrin-Binding Site Confirmed By Site-Directed Mutagenesis
المؤلفون: Renauld-Mongenie, G., Lins, Laurence, Krell, T., Laffly, L., Mignon, M., Dupuy, M., Delrue, Rm., Guinet-Morlot, F., Brasseur, Robert, Lissolo, L.
المصدر: Journal of Bacteriology, 186 (3), 850-857 (2004)
بيانات النشر: American Society for Microbiology, 2004.
سنة النشر: 2004
مصطلحات موضوعية: Life sciences, Biochemistry, biophysics & molecular biology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire
الوصف: A sequence-based prediction method was employed to identify three ligand-binding domains in transferrin-binding protein B (TbpB) of Neisseria meningitidis strain B16B6. Site-directed mutagenesis of residues located in these domains has led to the identification of two domains, amino acids 53 to 57 and 240 to 245, which are involved in binding to human transferrin (htf). These two domains are conserved in an alignment of different TbpB sequences from N. meningitidis and Neisseria gonorrhoeae, indicating a general functional role of the domains. Western blot analysis and BIAcore and isothermal titration calorimetry experiments demonstrated that site-directed mutations in both binding domains led to a decrease or abolition of htf binding. Analysis of mutated proteins by circular dichroism did not provide any evidence for structural alterations due to the amino acid replacements. The TbpB mutant R243N was devoid of any htf-binding activity, and antibodies elicited by the mutant showed strong bactericidal activity against the homologous strain, as well as against several heterologous tbpB isotype I strains.
نوع الوثيقة: journal article
http://purl.org/coar/resource_type/c_6501
article
اللغة: English
Relation: urn:issn:0021-9193; urn:issn:1098-5530
DOI: 10.1128/JB.186.3.850-857.2004
URL الوصول: https://orbi.uliege.be/handle/2268/63523
حقوق: restricted access
http://purl.org/coar/access_right/c_16ec
info:eu-repo/semantics/restrictedAccess
رقم الأكسشن: edsorb.63523
قاعدة البيانات: ORBi
الوصف
DOI:10.1128/JB.186.3.850-857.2004