A comparison of the immunogenicity of a pair of enantiomeric proteins

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Abstract
The immunogenicity of a folded, all D‐amino acid protein‐ rubredoxin, has been compared with that for the corresponding L‐protein enantiomer. Following multiple administrations with alum adjuvant, the L‐protein induced a strong, specific lgG antibody response, whereas the D‐protein did not. This relative lack of responsiveness to the D‐protein cannot be attributed to rapid excretion, since it is retained at least 4 times longer than the natural L‐protein. These observations provide the first direct evidence that a folded D‐amino acid protein has low immunogenicity and is long lived in vivo. Proteins with such properties may be useful as molecular platforms in a variety of chemical and pharmaco‐logical applications.