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Salvador Eugenio C Caoili - One of the best experts on this subject based on the ideXlab platform.

  • expressing redundancy among linear epitope sequence data based on residue level physicochemical similarity in the context of antigenic Cross Reaction
    Advances in Bioinformatics, 2016
    Co-Authors: Salvador Eugenio C Caoili
    Abstract:

    Epitope-based design of vaccines, immunotherapeutics, and immunodiagnostics is complicated by structural changes that radically alter immunological outcomes. This is obscured by expressing redundancy among linear-epitope data as fractional sequence-alignment identity, which fails to account for potentially drastic loss of binding affinity due to single-residue substitutions even where these might be considered conservative in the context of classical sequence analysis. From the perspective of immune function based on molecular recognition of epitopes, functional redundancy of epitope data (FRED) thus may be defined in a biologically more meaningful way based on residue-level physicochemical similarity in the context of antigenic Cross-Reaction, with functional similarity between epitopes expressed as the Shannon information entropy for differential epitope binding. Such similarity may be estimated in terms of structural differences between an immunogen epitope and an antigen epitope with reference to an idealized binding site of high complementarity to the immunogen epitope, by analogy between protein folding and ligand-receptor binding; but this underestimates potential for Cross-reactivity, suggesting that epitope-binding site complementarity is typically suboptimal as regards immunologic specificity. The apparently suboptimal complementarity may reflect a tradeoff to attain optimal immune function that favors generation of immune-system components each having potential for Cross-reactivity with a variety of epitopes.

  • expressing redundancy among linear epitope sequence data based on residue level physicochemical similarity in the context of antigenic Cross Reaction
    Advances in Bioinformatics, 2016
    Co-Authors: Salvador Eugenio C Caoili
    Abstract:

    Epitope-based design of vaccines, immunotherapeutics, and immunodiagnostics is complicated by structural changes that radically alter immunological outcomes. This is obscured by expressing redundancy among linear-epitope data as fractional sequence-alignment identity, which fails to account for potentially drastic loss of binding affinity due to single-residue substitutions even where these might be considered conservative in the context of classical sequence analysis. From the perspective of immune function based on molecular recognition of epitopes, functional redundancy of epitope data (FRED) thus may be defined in a biologically more meaningful way based on residue-level physicochemical similarity in the context of antigenic Cross-Reaction, with functional similarity between epitopes expressed as the Shannon information entropy for differential epitope binding. Such similarity may be estimated in terms of structural differences between an immunogen epitope and an antigen epitope with reference to an idealized binding site of high complementarity to the immunogen epitope, by analogy between protein folding and ligand-receptor binding; but this underestimates potential for Cross-reactivity, suggesting that epitope-binding site complementarity is typically suboptimal as regards immunologic specificity. The apparently suboptimal complementarity may reflect a tradeoff to attain optimal immune function that favors generation of immune-system components each having potential for Cross-reactivity with a variety of epitopes.

R Soloeta - One of the best experts on this subject based on the ideXlab platform.

T Fenyvesi - One of the best experts on this subject based on the ideXlab platform.

J J Goday - One of the best experts on this subject based on the ideXlab platform.

Zouhair M Atassi - One of the best experts on this subject based on the ideXlab platform.

  • Cross Reaction of tetanus and botulinum neurotoxins a and b and the boosting effect of botulinum neurotoxins a and b on a primary anti tetanus antibody response
    Immunological Investigations, 2002
    Co-Authors: Behzod Z Dolimbek, Joseph Jankovic, Zouhair M Atassi
    Abstract:

    The present studies were carried out in order to investigate the Cross-Reaction of botulinum neurotoxins (BoNTs) with human and mouse antibodies against tetanus neurotoxin (TeNT) and determine whether injection of BoNT into a host that has been primed with TeNT would result in boosting of the response to the injected BoNT. Human antisera against TeNT obtained from 9 individuals were found to exhibit substantial Cross-Reaction with BoNTs A and B. We prepared antibodies (Abs) against inactivated tetanus neurotoxin (TeNT) in outbred mice and determined the binding of these Abs to active TeNT and active botulinum neurotoxins (BoNTs) A and B. Blood samples were collected before immunization (day 0) and on days 42, 82 and 125 after the first injection. The Reactions of these sera with the immunizing antigen (inactivated TeNT), active TeNT, active BoNT/A and active BoNT/B were determined. At a fixed dilution (1:62.5 v/v), the sera contained high levels of Abs that reacted with TeNT and also with BoNTs A and B. T...