Influence of oxidation and multimerization on the immunogenicity of a thioredoxin-l2 prophylactic papillomavirus vaccine.

Epitope-specific mAb bound equally to a reduced or oxidized construct of three tandemly repeated copies of peptide HPV 16 (20-38) L2 separated from each other by a GGP spacer sequence and fused to bacterial thioredoxin. The authors conclude that disulfide bonds are not an absolute requirement for recognition but contribute to binding.