Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1997-11-4
pubmed:abstractText
Transferrin-binding protein B (TbpB) from Neisseria meningitidis binds human transferrin (hTf) at the surface of the bacterial cell as part of the iron uptake process. To identify hTf binding sites within the meningococcal TbpB, defined regions of the molecule were produced in Escherichia coli by a translational fusion expression system and the ability of the recombinant proteins (rTbpB) to bind peroxidase-conjugated hTf was characterized by Western blot and dot blot assays. Both the N-terminal domain (amino acids [aa] 2 to 351) and the C-terminal domain (aa 352 to 691) were able to bind hTf, and by a peptide spot synthesis approach, two and five hTf binding sites were identified in the N- and C-terminal domains, respectively. The hTf binding activity of three rTbpB deletion variants constructed within the central region (aa 346 to 543) highlighted the importance of a specific peptide (aa 377 to 394) in the ligand interaction. Taken together, the results indicated that the N- and C-terminal domains bound hTf approximately 10 and 1000 times less, respectively, than the full-length rTbpB (aa 2 to 691), while the central region (aa 346 to 543) had a binding avidity in the same order of magnitude as the C-terminal domain. In contrast with the hTf binding in the N-terminal domain, which was mediated by conformational epitopes, linear determinants seemed to be involved in the hTf binding in the C-terminal domain. The host specificity for transferrin appeared to be mediated by the N-terminal domain of the meningococcal rTbpB rather than the C-terminal domain, since we report that murine Tf binds to the C-terminal domain. Antisera raised to both N- and C-terminal domains were bactericidal for the parent strain, indicating that both domains are accessible at the bacterial surface. We have thus identified hTf binding sites within each domain of the TbpB from N. meningitidis and propose that the N- and C-terminal domains together contribute to the efficient binding of TbpB to hTf with their respective affinities and specificities for determinants of their ligand.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-1487730, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-1639494, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-2110858, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-2151461, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-3132585, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-3881765, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-388439, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-3961484, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-6445876, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-6833213, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7558290, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7590185, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7789801, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7868605, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7890373, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-7928990, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8125919, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8132473, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8195069, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8256502, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8319895, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8344530, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8361358, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8423101, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8557646, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8631722, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8722096, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8821649, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8821945, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8890905, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-8975892, http://linkedlifedata.com/resource/pubmed/commentcorrection/9335289-9009351
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9193
pubmed:author
pubmed:issnType
Print
pubmed:volume
179
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6400-7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:9335289-Animals, pubmed-meshheading:9335289-Antibodies, Bacterial, pubmed-meshheading:9335289-Bacterial Outer Membrane Proteins, pubmed-meshheading:9335289-Binding Sites, pubmed-meshheading:9335289-Carrier Proteins, pubmed-meshheading:9335289-Escherichia coli, pubmed-meshheading:9335289-Humans, pubmed-meshheading:9335289-Immunoblotting, pubmed-meshheading:9335289-Iron-Binding Proteins, pubmed-meshheading:9335289-Neisseria meningitidis, pubmed-meshheading:9335289-Protein Conformation, pubmed-meshheading:9335289-Rabbits, pubmed-meshheading:9335289-Recombinant Fusion Proteins, pubmed-meshheading:9335289-Species Specificity, pubmed-meshheading:9335289-Transferrin, pubmed-meshheading:9335289-Transferrin-Binding Protein B, pubmed-meshheading:9335289-Transferrin-Binding Proteins
pubmed:year
1997
pubmed:articleTitle
Identification of human transferrin-binding sites within meningococcal transferrin-binding protein B.
pubmed:affiliation
Pasteur Mérieux Connaught, Marcy l'Etoile, France.
pubmed:publicationType
Journal Article