Bacteria targeted by human natural antibodies using α-Gal conjugated receptor-specific glycopolymers

被引:58
作者
Li, J [1 ]
Zacharek, S [1 ]
Chen, X [1 ]
Wang, JQ [1 ]
Zhang, W [1 ]
Janczuk, A [1 ]
Wang, PG [1 ]
机构
[1] Wayne State Univ, Dept Chem, Detroit, MI 48202 USA
基金
美国国家科学基金会;
关键词
alpha-Gal epitope; chemoenzymatic synthesis; bacteria; human natural anti-Gal antibodies;
D O I
10.1016/S0968-0896(99)00099-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Synthesis of polymerizable beta-lactosyl, Gal alpha 1-->3Gal and alpha-mannosyl acrylamide derivatives with either a hydrophobic aromatic spacer or a hydrophilic biocompatible oligoethoxyl spacer was accomplished. Radical terpolymerizations of beta-lactosyl monomer, alpha-mannosyl monomer, and acrylamide were conducted in aqueous media with ammonium persulfate and N,N,N,N'-tetramethylethylenediamine as initiators. The resulting water soluble glycopolymers were further transformed efficiently by a recombinant alpha 1-->3 galactosyltransferase to afford mediators bearing Gal alpha 1-->3Gal termini as xenoactive antigens and alpha-mannosyl termini as specific ligands for bacterial cells. The binding of the resulting multivalent glycopolymer to bacteria was tested by its ability to inhibit agglutination of yeast to E. coli. The binding of human natural anti-Gal antibodies to the alpha-Gal containing glycopolymers and a monovalent alpha-Gal-Man glycoconjugate was demonstrated by an ELISA inhibition assay. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:1549 / 1558
页数:10
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