Synthesis and Comparison of Antibody Recognition of Conjugates Containing Herpes Simplex Virus Type 1 Glycoprotein D Epitope VII1
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- 作者：Gá ; bor Mezö ; Eliandre de Oliveira ; Dimitrios Krikorian ; Matty Feijlbrief ; Annamá ; ria Jakab ; Vassilios Tsikaris ; Constantinos Sakarellos ; Sytske Welling-Wester ; David Andreu ; and Feren
- 刊名：Bioconjugate Chemistry
- 出版年：2003
- 出版时间：November 2003
- 年：2003
- 卷：14
- 期：6
- 页码：1260 - 1269
- 全文大小：133K
- 年卷期：v.14,no.6(November 2003)
- ISSN：1520-4812
文摘
Synthetic oligopeptides comprising linear or continuous topographic B-cell epitope sequences of proteinsmight be considered as specific and small size antigens. It has been demonstrated that the strengthand specificity of antibody binding could be altered by conjugation to macromolecules or by modificationin the flanking regions. However, no systematic studies have been reported to describe the effect ofdifferent carrier macromolecules in epitope conjugates. To this end, the influence of carrier structureand topology on antibody recognition of attached epitope has been studied by comparing the antibodybinding properties of a new set of conjugates with tetratuftsin analogue (H-[Thr-Lys-Pro-Lys-Gly]4-NH2, T20) sequential oligopeptide carrier (SOCn), branched chain polypeptide, poly[Lys(Seri-DL-Alam)](SAK), multiple antigenic peptide (MAP), and keyhole limpet hemocyanine (KLH). In these novelconstructs, peptide 9LKNleADPNRFRGKDL22 ([Nle11]-9-22) representing an immunodominant B cellepitope of herpes simplex virus type 1 glycoprotein D (HSV-1 gD) was conjugated to polypeptidesthrough a thioether or amide bond. Here we report on the preparation of sequential and polymericpolypeptides possessing chloroacetyl groups in multiple copies at the 
- and/or 
-amino group of thepolypeptides and its use for the conjugation of epitope peptides possessing Cys at C-terminal position.We have performed binding studies (direct and competitive ELISA) with monoclonal antibody (Mab)A16, recognizing the HSV gD-related epitope, [Nle11]-9-22, and conjugates containing identical anduniformly oriented epitope peptide in multiple copies attached to five different macromolecules ascarrier. Data suggest that the chemical nature of the carrier and the degree of substitution havemarked influence on the strength of antibody binding.
- and/or -amino group of thepolypeptides and its use for the conjugation of epitope peptides possessing Cys at C-terminal position.We have performed binding studies (direct and competitive ELISA) with monoclonal antibody (Mab)A16, recognizing the HSV gD-related epitope, [Nle11]-9-22, and conjugates containing identical anduniformly oriented epitope peptide in multiple copies attached to five different macromolecules ascarrier. Data suggest that the chemical nature of the carrier and the degree of substitution havemarked influence on the strength of antibody binding.