Cyclic disulfide model of the major antigenic site of serotype‐C foot‐and‐mouth disease virus

FEBS Letters

Cairó, Jordi J.²  Andreu, David²  Mateu, Mauricio G.¹  Giralt, Ernest²  Domingo, Esteban¹  Camarero, Julio A.² 

[1] Centro de Biología Molecular (CSIC-UAM), Cantoblanco, E-28049 Madrid, Spain;Department of Organic Chemistry, University of Barcelona, E-08028 Barcelona, Spain

关键词: Antigenic peptide;    Conformational restriction;    Circular dichroism;    Monoclonal antibody;    Solid phase peptide syntesis;   

DOI  :  10.1016/0014-5793(93)80985-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A cyclic disulfide peptide representing antigenic site A of foot-and-mouth-disease virus (FMDV) strain C-S8cl (residues 134 to 155 of viral protein l (VP1) with Tyr¹³⁶ and Arg¹⁵³ replaced by cystine; TTCTASARGDLAHLTTTHACHL) was synthesized by solid phase methods. Formation of the cyclic disulfide was carried out by air oxidation of the fully deprotected and reduced bis-cysteine precursor, under high dilution conditions. The identity of the cyclic peptide was confirmed by both physical and enzymatic methods. A conformational study of the cyclic peptide and of its linear parent structure (YTASARGDLAHLTTTHARHLP, residues 136–156 of VP1 of FMDV C-S8cl) by circular dichroism in the presence of a structure-inducing solvent showed the cyclic disulfide analog to adopt lower levels of α-helix than its linear counterpart. In competitive ELISA assays both peptides reacted with similar affinity against a representative panel of neutralizing monoclonal antibodies directed towards antigenic site A. Thus, a high inherent flexibility of this loop may preclude a conformational restriction strong enough to alter recognition by anti-virus antibodies.

【 授权许可】

Unknown