scholarly journals Delineating the regions of human transferrin involved in interactions with transferrin binding protein B from Neisseria meningitidis

2010 ◽  
Vol 77 (5) ◽  
pp. 1301-1314 ◽  
Author(s):  
Jessmi M. L. Ling ◽  
Collin H. Shima ◽  
David C. Schriemer ◽  
Anthony B. Schryvers
Keyword(s):  
Neisseria Meningitidis ◽  
Binding Protein ◽  
Human Transferrin ◽  
Protein B

scholarly journals Transferrin-Binding Protein B of Neisseria meningitidis: Sequence-Based Identification of the Transferrin-Binding Site Confirmed by Site-Directed Mutagenesis

2004 ◽  
Vol 186 (3) ◽  
pp. 850-857 ◽  
Author(s):  
Geneviève Renauld-Mongénie ◽  
Laurence Lins ◽  
Tino Krell ◽  
Laure Laffly ◽  
Michèle Mignon ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Binding Protein ◽  
Prediction Method ◽  
Binding Activity ◽  
Site Directed Mutagenesis ◽  
Titration Calorimetry ◽  
Directed Mutagenesis ◽  
Binding Domains ◽  
Homologous Strain ◽  
Protein B

ABSTRACT 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.

scholarly journals Purified meningococcal transferrin-binding protein B interacts with a secondary, strain-specific, binding site in the N-terminal lobe of human transferrin

1999 ◽  
Vol 339 (1) ◽  
pp. 143 ◽  
Author(s):  
Ian C. BOULTON ◽  
Andrew R. GORRINGE ◽  
Beatrice GORINSKY ◽  
Mark D. RETZER ◽  
Anthony B. SCHRYVERS ◽  
...  
Keyword(s):  
Binding Site ◽  
Specific Binding ◽  
Binding Protein ◽  
Human Transferrin ◽  
Protein B

scholarly journals Peptide-Peptide Interactions between Human Transferrin and Transferrin-Binding Protein B from Moraxellacatarrhalis

2003 ◽  
Vol 185 (8) ◽  
pp. 2603-2610 ◽  
Author(s):  
Kurtis L. Sims ◽  
Anthony B. Schryvers
Keyword(s):  
Synthetic Peptide ◽  
Structural Model ◽  
Binding Protein ◽  
Bacterial Species ◽  
Peptide Library ◽  
Human Transferrin ◽  
Peptide Interactions ◽  
Binding Peptides ◽  
Individual Peptide ◽  
Protein B

ABSTRACT Transferrin-binding protein B (TbpB) is one component of a bipartite receptor in several gram-negative bacterial species that binds host transferrin and mediates the uptake of iron for growth. Transferrin and TbpB are both bilobed proteins, and the interaction between these proteins seems to involve similar lobe-lobe interactions. Synthetic overlapping peptide libraries representing the N lobe of TbpB from Moraxella catarrhalis were prepared and probed with labeled human transferrin. Transferrin-binding peptides were localized to six different regions of the TbpB N lobe, and reciprocal experiments identified six different regions of the C lobe of transferrin that bound TbpB. Truncations of the N lobe of TbpB that sequentially removed each transferrin-binding determinant were used to probe an overlapping peptide library of the C lobe of human transferrin. The removal of each TbpB N-lobe transferrin-binding determinant resulted in a loss of reactivity with peptides from the synthetic peptide library representing the C lobe of transferrin. Thus, individual peptide-peptide interactions between ligand and receptor were identified. A structural model of human transferrin was used to map surface regions capable of binding to TbpB.

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