Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten

Conjugation chemistry does not always provide adequate spatial orientation of hapten in immunogens for the best presentation of generic or individual epitopes. In the present study, the influence of unique and multiple orientations of immunizing hapten on the immune response repertoire was compared...

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Main Authors: Maksim A. Burkin, Inna A. Galvidis, Sergei A. Eremin
Format: Article
Language:English
Published: MDPI AG 2019-04-01
Series:Biosensors
Subjects:
Online Access:https://www.mdpi.com/2079-6374/9/2/52
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author Maksim A. Burkin
Inna A. Galvidis
Sergei A. Eremin
author_facet Maksim A. Burkin
Inna A. Galvidis
Sergei A. Eremin
author_sort Maksim A. Burkin
collection DOAJ
description Conjugation chemistry does not always provide adequate spatial orientation of hapten in immunogens for the best presentation of generic or individual epitopes. In the present study, the influence of unique and multiple orientations of immunizing hapten on the immune response repertoire was compared to select generic recognition system. The glycopeptides, teicoplanin (TPL) and ristomycin (RSM), were conjugated to BSA to produce immunogens with unique and multiple orientations of haptens. Polyclonal antibodies generated against TPL conjugated through a single site were of uniform specificity and demonstrated selective TPL recognition, regardless of the coating conjugates design. The sensitivity (IC<sub>50</sub>) of 4 enzyme-linked immunosorbent assays (ELISAs) for TPL varied little within the 3.5&#8211;7.4 ng/mL, with a dynamic range of 0.2&#8211;100 ng/mL. RSM was coupled to BSA through several glycoside sites that evoked a wider repertoire of response. This first described anti-RSM antibody was selective for RSM in homologous hapten-coated ELISAs with IC<sub>50</sub> values in the range 4.2&#8211;35 ng/mL. Among the heterologous antigens, periodate-oxidized TPL conjugated to gelatine was selected as the best binder of generic anti-RSM fraction. The developed ELISA showed group recognition of glycopeptides RSM, TPL, eremomycin, and vancomycin with cross-reactivity of 37&#8211;100% and a 10&#8211;10,000 ng/mL dynamic range. Thus, multiple presentations of immunizing hapten help expand the repertoire of immune responses and opportunities for the selection of the required fine-specificity agent.
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spelling doaj.art-44e545a4f1604950b1bd1f3900fcbda32022-12-22T02:55:56ZengMDPI AGBiosensors2079-63742019-04-01925210.3390/bios9020052bios9020052Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of HaptenMaksim A. Burkin0Inna A. Galvidis1Sergei A. Eremin2Immunology Department, I. Mechnikov Research Institute for Vaccines and Sera, 105064 Moscow, RussiaImmunology Department, I. Mechnikov Research Institute for Vaccines and Sera, 105064 Moscow, RussiaFaculty of Chemistry, M. V. Lomonosov MSU, Leninsky Gory, 1, 119991 Moscow, RussiaConjugation chemistry does not always provide adequate spatial orientation of hapten in immunogens for the best presentation of generic or individual epitopes. In the present study, the influence of unique and multiple orientations of immunizing hapten on the immune response repertoire was compared to select generic recognition system. The glycopeptides, teicoplanin (TPL) and ristomycin (RSM), were conjugated to BSA to produce immunogens with unique and multiple orientations of haptens. Polyclonal antibodies generated against TPL conjugated through a single site were of uniform specificity and demonstrated selective TPL recognition, regardless of the coating conjugates design. The sensitivity (IC<sub>50</sub>) of 4 enzyme-linked immunosorbent assays (ELISAs) for TPL varied little within the 3.5&#8211;7.4 ng/mL, with a dynamic range of 0.2&#8211;100 ng/mL. RSM was coupled to BSA through several glycoside sites that evoked a wider repertoire of response. This first described anti-RSM antibody was selective for RSM in homologous hapten-coated ELISAs with IC<sub>50</sub> values in the range 4.2&#8211;35 ng/mL. Among the heterologous antigens, periodate-oxidized TPL conjugated to gelatine was selected as the best binder of generic anti-RSM fraction. The developed ELISA showed group recognition of glycopeptides RSM, TPL, eremomycin, and vancomycin with cross-reactivity of 37&#8211;100% and a 10&#8211;10,000 ng/mL dynamic range. Thus, multiple presentations of immunizing hapten help expand the repertoire of immune responses and opportunities for the selection of the required fine-specificity agent.https://www.mdpi.com/2079-6374/9/2/52hapten conjugate designantibody repertoiregroup recognitionristomycinteicoplanineremomycinvancomycin
spellingShingle Maksim A. Burkin
Inna A. Galvidis
Sergei A. Eremin
Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
Biosensors
hapten conjugate design
antibody repertoire
group recognition
ristomycin
teicoplanin
eremomycin
vancomycin
title Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
title_full Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
title_fullStr Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
title_full_unstemmed Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
title_short Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
title_sort specific and generic immunorecognition of glycopeptide antibiotics promoted by unique and multiple orientations of hapten
topic hapten conjugate design
antibody repertoire
group recognition
ristomycin
teicoplanin
eremomycin
vancomycin
url https://www.mdpi.com/2079-6374/9/2/52
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AT innaagalvidis specificandgenericimmunorecognitionofglycopeptideantibioticspromotedbyuniqueandmultipleorientationsofhapten
AT sergeiaeremin specificandgenericimmunorecognitionofglycopeptideantibioticspromotedbyuniqueandmultipleorientationsofhapten