Antibody reactivity of conformational peptide mimics of a conserved H5N1 neutralization site in different fusion proteins

Antibody reactivity of conformational peptide mimics of a conserved H5N1 neutralization site in... Several peptide mimics of a conserved H5N1 avian influenza virus neutralization site recognized by 8H5 mAb have been reported previously. In this study, the secondary and possibly higher structural orders of the peptide mimics 122 and 125 were investigated and found to be closely related to the specific binding with 8H5 mAb. These two peptide mimics were fused to three different carrier proteins, and the antibody binding activities were recovered in 4 of the 11 fusion proteins. HEV structural protein p239 and HBc were more suitable than the outer membrane protein T47 of the Treponema pallidum particle for the recovery of reactivity. The increase in the copy number of peptide mimics was important for the recovery of antibody-binding activity and the interaction between peptide and carrier protein may affect the spatial structure of both the peptide and the carrier protein. These results are likely to be of relevance for conformational peptide mimics in diagnostic tests, vaccine and inhibitors. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Antibody reactivity of conformational peptide mimics of a conserved H5N1 neutralization site in different fusion proteins

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Publisher
Springer Vienna
Copyright
Copyright © 2010 by Springer-Verlag
Subject
Biomedicine; Infectious Diseases; Medical Microbiology ; Virology
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-009-0542-2
Publisher site
See Article on Publisher Site

Abstract

Several peptide mimics of a conserved H5N1 avian influenza virus neutralization site recognized by 8H5 mAb have been reported previously. In this study, the secondary and possibly higher structural orders of the peptide mimics 122 and 125 were investigated and found to be closely related to the specific binding with 8H5 mAb. These two peptide mimics were fused to three different carrier proteins, and the antibody binding activities were recovered in 4 of the 11 fusion proteins. HEV structural protein p239 and HBc were more suitable than the outer membrane protein T47 of the Treponema pallidum particle for the recovery of reactivity. The increase in the copy number of peptide mimics was important for the recovery of antibody-binding activity and the interaction between peptide and carrier protein may affect the spatial structure of both the peptide and the carrier protein. These results are likely to be of relevance for conformational peptide mimics in diagnostic tests, vaccine and inhibitors.

Journal

Archives of VirologySpringer Journals

Published: Jan 1, 2010

References

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