Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies.

@article{Harris1997ExploringTB,
  title={Exploring the basis of peptide-carbohydrate crossreactivity: evidence for discrimination by peptides between closely related anti-carbohydrate antibodies.},
  author={Shannon L. Harris and L Craig and Jarnail Mehroke and Mohamad Rashed and Michael B. Zwick and K Kenar and Eric J. Toone and Neil S. Greenspan and France-Isabelle Auzanneau and J. R. Marino-albernas and B. Mario Pinto and Jamie K. Scott},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1997},
  volume={94 6},
  pages={
          2454-9
        }
}
  • S. Harris, L. Craig, J. Scott
  • Published 18 March 1997
  • Biology
  • Proceedings of the National Academy of Sciences of the United States of America
To investigate the molecular basis of antigenic mimicry by peptides, we studied a panel of closely related mAbs directed against the cell-wall polysaccharide of group A Streptococcus. These antibodies have restricted V-gene usage, indicating a shared mechanism of binding to a single epitope. Epitope mapping studies using synthetic fragments of the cell-wall polysaccharide supported this conclusion. All of the mAbs isolated crossreactive peptides from a panel of phage-displayed libraries, and… 
All-D peptides recognized by an anti-carbohydrate antibody identified from a positional scanning library.
TLDR
The study of immune recognition using combinatorial chemistry may offer new insights into the molecular basis of cross-reactivity in monoclonal antibodies.
Peptide Mimicry of Streptococcal Group A Carbohydrate
TLDR
This chapter explores the immunochemical relationships, as defined by antibodies, between the cell wall polysaccharide of Streptococcus pyogenes (group A streptococci) and peptides and investigates peptide mimicry of GAC with respect to five GAC-specific monoclonal antibodies.
A Molecular Basis for Functional Peptide Mimicry of a Carbohydrate Antigen*
TLDR
A molecular perspective for peptide mimicry is established by comparing the three-dimensional basis of BR55-2 binding to LeY with the binding of the same antibodies to peptides, confirming that peptides and carbohydrates can bind to the same antibody-binding site and that peptide can structurally and functionally mimic salient features of carbohydrate epitopes.
Peptides that mimic the group B streptococcal type III capsular polysaccharide antigen.
TLDR
Data demonstrate that a peptide mimetic of the GBS capsular polysaccharide is both antigenic and immunogenic and the incorporation of such peptides into vaccine preparations may enhance the efficacy of vaccines in inducing Ab responses to important carbohydrate epitopes.
Plasticity within the Antigen-Combining Site May Manifest as Molecular Mimicry in the Humoral Immune Response1
TLDR
It is proposed that the degeneracy of specificity arising from the plasticity at the Ag-combining site in a subset of the Ab clones may be responsible for exhibiting molecular mimicry in the context of Ab response.
Toward a Better Understanding of the Basis of the Molecular Mimicry of Polysaccharide Antigens by Peptides
TLDR
Using NMR-derived pentasaccharide and peptide conformations coupled to STD information, models of antigen-antibody interaction were obtained and only one model was found compatible with experimental data when large O-SP fragments were docked into one of the mIgA-binding sites.
Directing the Immune Response to Carbohydrate Antigens*
TLDR
It is demonstrated that mimicry is based more upon functional rather than structural determinants that regulate mimeotope-induced T-dependent antibody responses to polysaccharide and emphasize that rational approaches can be employed to develop further vaccine candidates.
Towards the development of peptide mimotopes of carbohydrate antigens as cancer vaccines.
TLDR
These experiments suggest that peptide mimotopes of the LeY and sLeX tumor-associated carbohydrate antigen and QS-21 adjuvant could be considered as an immunogenic therapeutic vaccine in carcinoma and melanoma patients in the minimal residual disease setting.
...
...

References

SHOWING 1-10 OF 31 REFERENCES
Probing the basis of antibody reactivity with a panel of constrained peptide libraries displayed by filamentous phage.
TLDR
This work constructed and screened a panel of peptide libraries displayed by filamentous bacteriophage, whose sizes range from 150 million to 10 billion clones, and found cross-reactivity with peptides was always found for antibodies produced against peptides, linear epitopes on folded proteins and, surprisingly, carbohydrates.
Characterization of Shigella flexneri-specific murine monoclonal antibodies by chemically defined glycoconjugates.
Chemically defined glycoconjugates are demonstrated to have considerable potential for selecting hybridoma antibodies directed toward O-antigenic determinants, especially when used in combination
Monoclonal antibodies to streptococcal group A carbohydrate. I. A dominant idiotypic determinant is located on Vk.
TLDR
It appears that anti-GAC antibodies are composed of H chains bearing a few VH regions pairing with a few L chains, similar to previous estimates of clonal repertoires of approximately 200.
A family of concanavalin A-binding peptides from a hexapeptide epitope library.
TLDR
The results demonstrate that the specificity of Con A is not limited to carbohydrates and that highly selective sugar-mimics for lectins of plant, animal, or bacterial origin may be identified from epitope libraries.
Peptide libraries define the fine specificity of anti-polysaccharide antibodies to Cryptococcus neoformans.
TLDR
It is shown that peptide mimotopes for a complex microbial polysaccharide can be identified by screening phage peptide libraries and demonstrates the usefulness of such peptides in analyzing closely related interactive sites of proteins in general and of antibodies in particular.
Peptide mimicry of the meningococcal group C capsular polysaccharide.
TLDR
A synthetic peptide spanning the CDR3 domain was synthesized and complexed to proteosomes (meningococcal group B outer membrane protein) and immunizations of BALB/c mice with the peptide-proteosome complex resulted in a significant anti-MCP antibody response.
Evidence for the extended helical nature of polysaccharide epitopes. The 2.8 A resolution structure and thermodynamics of ligand binding of an antigen binding fragment specific for alpha-(2-->8)-polysialic acid.
TLDR
X-ray crystallographic and thermodynamic evidence are consistent with a binding site that accommodates at least eight sialic acid residues, and a model of antigen binding is presented that satisfies this thermodynamic data, as well as a previously reported requirement of conformational specificity of the oligosaccharide.
Molecular recognition of a Salmonella trisaccharide epitope by monoclonal antibody Se155-4.
TLDR
Detailed epitope mapping of the molecular recognition by modified and monodeoxy oligosaccharide derivatives showed that complementary surfaces and three antibody-saccharide hydrogen bonds are essential for full binding activity.
...
...