A comparison of the immunogenicity of a pair of enantiomeric proteins.
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 IgG 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 pharmacological applications.
Dintzis
H M
HM
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
Symer
D E
DE
Dintzis
R Z
RZ
Zawadzke
L E
LE
Berg
J M
JM
D000276:Adjuvants, Immunologic; D000534:Alum Compounds; D000818:Animals; D000917:Antibody Formation / Q000276:immunology; D005260:Female; D051379:Mice; D008815:Mice, Inbred Strains; D012416:Rubredoxins / Q000276:immunology* / Q000493:pharmacokinetics; D013237:Stereoisomerism; D013329:Structure-Activity Relationship
D000276:Adjuvants, Immunologic; D000534:Alum Compounds; D012416:Rubredoxins; C041524:aluminum sulfate