Cited by 104Monoclonal and Polyclonal Antibodies ResearchProtein Structure and Dynamicsvaccines and immunoinformatics approaches

A comparison of the immunogenicity of a pair of enantiomeric proteins

Dintzis, Howard M., Symer, David E., Dintzis, Renee Z., Zawadzke, Laura E., Berg, Jeremy M.·1993·Proteins: Structure, Function, and Bioinformatics

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. © 1993 Wiley‐Liss, Inc.

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Crossref · 10.1002/prot.340160309

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Authors
Dintzis, H. M., Symer, D. E., Dintzis, R. Z., Zawadzke, L. E., & Berg, J. M.
Affiliations
Johns Hopkins University (US)
Corresponding author
Dintzis, Howard M.
Venue
Proteins: Structure, Function, and Bioinformatics
Publisher
Wiley
Published
1993-07
Volume
16
Issue
3
Pages
306-308
ISSN
  • 0887-3585 (ISSN-L)
  • 1097-0134
OpenAlex
W2167125107
Cited by
104
References
13
Citations by year
2026: 8 · 2025: 5 · 2024: 9 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 4 · 2019: 6 · 2018: 5 · 2017: 2 · 2016: 4 · 2015: 4 · 2014: 4 · 2012: 3
FWCI
4.22
Type
journal article
Language
en
Open access
closed
Locations
  • Proteins Structure Function and Bioinformatics (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation
  • National Institutes of Health
Topics
  • Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
Keywords
rubredoxin, immunogenicity, IgG antibody response, alum adjuvant, protein excretion
MeSH terms
Adjuvants, Immunologic, Alum Compounds, Animals, Antibody Formation, Female, Mice, Inbred Strains, Rubredoxins, Stereoisomerism, Structure-Activity Relationship, Mice

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