Cyclic disulfide model of the major antigenic site of serotype-C foot-and-mouth disease virus
Autor: | Julio A. Camarero, Esteban Domingo, David Andreu, Jordi J. Cairó, Ernest Giralt, Mauricio G. Mateu |
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Rok vydání: | 1993 |
Předmět: |
Monoclonal antibody
Models Molecular Solid phase peptide syntesis Circular dichroism Protein Conformation Stereochemistry Viral protein medicine.drug_class Molecular Sequence Data Biophysics Cystine Enzyme-Linked Immunosorbent Assay Peptide medicine.disease_cause Peptides Cyclic Biochemistry Epitopes Mice Viral Proteins chemistry.chemical_compound Aphthovirus Antigenic peptide Structural Biology Genetics medicine Animals Amino Acid Sequence Disulfides Serotyping Molecular Biology chemistry.chemical_classification biology Chemistry Circular Dichroism Antibodies Monoclonal Cell Biology biology.organism_classification Peptide Fragments Cyclic peptide Conformational restriction Foot-and-mouth disease virus |
Zdroj: | FEBS Letters. 328:159-164 |
ISSN: | 0014-5793 |
Popis: | 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. |
Databáze: | OpenAIRE |
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