A COMPARISON OF THE IMMUNOGENICITY OF A PAIR OF ENANTIOMERIC PROTEINS

被引：93

作者：

DINTZIS, HM ^{[1
]}

SYMER, DE ^{[1
]}

DINTZIS, RZ ^{[1
]}

ZAWADZKE, LE ^{[1
]}

BERG, JM ^{[1
]}

机构：

[1] JOHNS HOPKINS UNIV,SCH MED,DEPT CELL BIOL & ANAT,BALTIMORE,MD 21205

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1993年 / 16卷 / 03期

关键词：

RUBREDOXIN; IGG ANTIBODY; IGM ANTIBODY; IMMUNOGEN;

D O I：

10.1002/prot.340160309

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：306 / 308

页数：3