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A comparison of the immunogenicity of a pair of enantiomeric proteins
Author(s) -
Dintzis Howard M.,
Symer David E.,
Dintzis Renee Z.,
Zawadzke Laura E.,
Berg Jeremy M.
Publication year - 1993
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340160309
Subject(s) - immunogenicity , enantiomer , amino acid , chemistry , adjuvant , in vivo , antibody , biochemistry , biology , stereochemistry , immunology , genetics
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. © 1993 Wiley‐Liss, Inc.