Key result
Synthetic foot-and-mouth VP1 peptides display helix-forming properties linked to crossreactivity and position 148 substitutions.
Why the study?
The structural basis of antigenic variation in foot-and-mouth disease virus serotype A12, particularly involving residues 148 and 153 in VP1, was not fully understood.
Population
Seven antigenic variants from a single field isolate of foot-and-mouth disease virus serotype A12
Comparison
Peptides with substitutions at residues 148 and 153 in VP1
Design
Molecular modeling, circular dichroism, and serological analysis
Authors
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May guide FMDV antigenic variant prediction; leaves open in vivo cross-protection and vaccine implications.
France et al. (1994) studied Foot-and-mouth disease virus. Synthetic peptides corresponding to the region 141-160 of viral protein VP1 was evaluated on Helix-forming properties and serological crossreactivities. Synthetic peptides of foot-and-mouth disease virus VP1 display helix-forming properties that correlate with serological crossreactivities and are highly sensitive to substitutions at position 148.
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