酶谱凝胶中和革兰氏阴性菌组成型β -内酰胺酶的免疫学比较:抗tem -1和抗tem -2血清的特性。

G Paul, M Barthélémy, A Philippon, J Peduzzi, L Gilly, R Labia, P Névot
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引用次数: 0

摘要

酶谱技术应用于抗tem -1和抗tem -2血清的β -内酰胺酶中和试验。两者都含有针对革兰氏阴性细菌的各种β -内酰胺酶的中和抗体。定量中和允许分类为5组28 β -内酰胺酶作为标准和61从临床分离。首先是TEM-1和TEM-2酶,包括TLE-1、SHV-1、SHV-2,肺炎克雷伯菌青霉菌酶和CTX-1。部分中和区分了两组含有CARB组的酶,这两组酶不同于PSE-2和PSE-3,而malinea malonatica含有MAL青霉菌酶,这两组酶不同于L. amalonatica。广谱β -内酰胺酶构成了一组独特的部分中和酶。未被两种血清中和的β -内酰胺酶包括质粒介导的oxa酶、各种物种特异性β -内酰胺酶和头孢菌素酶。酶的抗原相似性似乎与它们的催化性质,即青霉菌酶的相似性程度有关。这种β -内酰胺酶群之间的比较为已建立的和最近进化的β -内酰胺酶的生理和结构分析提供了一种间接的方法。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Immunological comparison of constitutive beta-lactamases of gram-negative bacteria by neutralization in zymogram gels: properties of anti-TEM-1 and anti-TEM-2 sera.

The zymogram technique was applied to a beta-lactamase neutralization assay with anti-TEM-1 and anti-TEM-2 sera. Both were shown to contain neutralizing antibodies directed towards various beta-lactamases of Gram-negative bacteria. The quantitative neutralization allowed classification into five groups of the 28 beta-lactamases used as standards and 61 from clinical isolates. In the first were enzymes such as TEM-1 and TEM-2 including TLE-1, SHV-1, SHV-2, penicillinases of Klebsiella pneumoniae and CTX-1. Partial neutralization distinguished two groups containing the CARB group of enzymes, which are different from PSE-2 and PSE-3, and the MAL penicillinases of Levinea malonatica, which are different from L. amalonatica enzymes. Broad spectrum beta-lactamases of K. oxytoca constituted a unique group of partially neutralized enzymes. Among the beta-lactamases not neutralized by either serum were the plasmid-mediated OXA-enzymes, various species-specific beta-lactamases and cephalosporinases. The antigenic similarities of the enzymes appeared to correlate with the extent of similarities of their catalytic properties, namely those of penicillinases. Such comparisons between the beta-lactamase groups provide an indirect approach to the physiological and structural analysis of established and recently evolved beta-lactamases.

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