التفاصيل البيبلوغرافية
| العنوان: |
Molecular characterization of hybrid Tbp2 proteins from Neisseria meningitidis. |
| المؤلفون: |
Legrain, Michèle, Findeli, Annie, Villeval, Dominique, Quentin-Millet, Marie-José, Jacobs, Eric |
| المصدر: |
Molecular Microbiology; Jan1996, Vol. 19 Issue 1, p159-169, 11p, 4 Diagrams, 1 Graph |
| مصطلحات موضوعية: |
TRANSFERRIN, CARRIER proteins, LIPOPROTEINS, IMMUNE system, AMINO acids |
| مستخلص: |
Transferrin-binding protein 2 (Tbp2) from Neisseria is an outer membrane-associated extracellular lipoprotein that is involved in iron capture within the infected host. The analysis of tbp2 clones isolated from various bacterial strains revealed extensive divergences throughout the open reading frame (ORF), with predicted amino acid (aa) sequences displaying 47% to 83% identity. Such a variability is likely to have resulted from the selective pressure exerted by the host immune system, but raises questions regarding the existing constraints for conservation of protein function. Indeed, the neisserial Tbp2s include a large structured domain, extending throughout the N-terminal half of the protein (~270-290 aa), which is extremely stable and whose conformational integrity is required for efficient binding to human transferrin (hTf). In this work, a functional study of Tbp2s encoded by hybrid genes constructed by reassorting highly divergent tbp2 sequences in the region of the ORF encoding this structured domain was performed. The data demonstrate that the determinant intramolecular interactions allowing formation of a stable Tbp2 structure able to interact efficiently with hTf or/and that the Tbp2 residues involved in the interaction with hTf are not well conserved. However, a number of rearrangements appeared to generate genes encoding proteins which have retained structural stability and hTf-binding capacity. This suggested that despite the extreme aa sequence divergence and the conformational constraints, horizontal genetic exchanges, which are known to occur in neisserial populations, may have contributed significantly to the generation of sequence variation within tbp2 ORFs. The analysis of two tbp2 clones characterized in this work supports this hypothesis. [ABSTRACT FROM AUTHOR] |
|
Copyright of Molecular Microbiology is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| قاعدة البيانات: |
Complementary Index |
