Topological mimicry of cross-reacting enantiomeric peptide antigens
Open accessAbstract
Rabbit polyclonal antibodies against multimeric peptide antigens were found to cross-react to a significant extent with topologically related variants of the parent antigen, where the chirality of each amino acid residue (inverso derivatives), or the peptide sequence orientation (retro derivatives), was inverted or where both modifications were simultaneously introduced (retro-inverso derivatives). All peptide variants displayed similar recognition properties for antibodies and similar dose-dependent inhibitory effects on the interaction between immobilized parent antigen and corresponding antibodies. Importance of peptide side chain topology on antigenicity was evaluated analyzing the recognition properties of two sequence-simplified parent peptide variants, one lacking of the side chains in the sequence odd position and the other in even position. These two variants, prepared introducing glycine residues alternatively in the parent peptide sequence, were found to cross-react to a significant extent with the original antibody raised against the parent peptide. Analysis of molecular models of peptide enantiomeric variants in the elongated all-trans configuration suggested that the topological equivalence of alternating side chains could lead to the formation of similar recognition surfaces, thus mimicking the parent peptide antigenic structure.
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The final production yield of anti-HER2 scFv was 147 mg/L under optimal expression conditions (24 h after induction with 0.05 mM IPTG at 30 °C, LB medium, SHuffle strain).
“The final production yield of the anti-HER2 scFv was 147 mg/L, under optimal expression conditions (24 h after induction with 0.05 mM IPTG at 30 °C, LB medium, SHuffle strain).”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [111]
The Materials and Methods and Results passages describe synthetic peptide antigens and anti-MAP-P15 antibodies, not anti-HER2 scFv production. Searches for the 147 mg/L yield, SHuffle strain, IPTG induction, and the stated expression conditions found no passage addressing the claim. No page numbers were provided for these passages. (LLM, conf=0.78)
Experimental — accuracy not yet measuredExpression of an scFv against HER2 derived from Trastuzumab in SHuffle at 30 °C resulted in enhanced solubility and higher expression level compared to its expression in BL21(DE3) at 37 °C.
“Recently, it has been reported that the expression of an scFv against HER2 derived from Trastuzumab (drug bank number DB00072) in SHuffle at 30 °C resulted in enhanced solubility and a higher expression level of the molecule as compared to its expression in BL21 (DE3) at 37 °C [109,110,111,112].”
From Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments (2020) · cites this paper as [111]
The paper’s Results discuss antibody cross-recognition of P15 peptide variants, not recombinant scFv expression. Searches for trastuzumab, HER2, SHuffle, and BL21(DE3) found no passage addressing the claimed solubility or expression comparison. The available passages have no page numbers. (LLM, conf=0.78)
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Tam, J. P. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.15.5409 · Cited by 1,251 · see citing works
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Evolution of Escherichia coli Expression System in Producing Antibody Recombinant Fragments
Sandomenico, A., Sivaccumar, J. P., & Ruvo, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176324 · Cited by 134 · see citing works
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- Authors
- Verdoliva, A., Ruvo, M., Cassani, G., & Fassina, G.
- Corresponding author
- Fassina, Giorgio
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 51
- Pages
- 30422-30427
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2100671145
- Cited by
- 30
- References
- 1
- Citations by year
- 2022: 1 · 2021: 2 · 2020: 2 · 2018: 1 · 2015: 1
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chemical Synthesis and Analysis
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › vaccines and immunoinformatics approaches
- Keywords
- antibody-antigen recognition, chirality inversion, glycine substitution, peptidomimetics, molecular modeling, all-trans conformation, antigenicity
- MeSH terms
- Amino Acid Sequence, Animals, Antibodies, Antigen-Antibody Reactions, Antigens, Chromatography, Affinity, Cross Reactions, Glycine, Isomerism, Molecular Sequence Data, Peptides, Rabbits, Stereoisomerism
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