ANALYSIS OF GENES ENCODING D-ALANINE-D-ALANINE LIGASE-RELATED ENZYMES IN LEUCONOSTOC-MESENTEROIDES AND LACTOBACILLUS SPP

被引：52

作者：

ELISHA, BG ^{[1
]}

COURVALIN, P ^{[1
]}

机构：

[1] INST PASTEUR,CNRS,EP J0058,UNITE AGENTS ANTIBACTERIENS,F-75724 PARIS 15,FRANCE

来源：

GENE | 1995年 / 152卷 / 01期

基金：

英国医学研究理事会;

关键词：

RECOMBINANT DNA; CELL WALL; GLYCOPEPTIDE RESISTANCE; PEPTIDOGLYCAN SYNTHESIS;

D O I：

10.1016/0378-1119(94)00692-L

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

Degenerate oligodeoxyribonucleotides complementary to sequences encoding conserved amino acid (aa) motifs in D-alanine:D-alanine ligases (Ddl) were used to amplify approx. 600-bp fragments from glycopeptide-resistant strains of Leuconostoc mesenteroides (Lm), Lactobacillus plantarum, La. salivarius and La. confusus, and from a susceptible strain of La, leichmannii. Comparison of the deduced aa sequences of the PCR products revealed that the Ddl-related enzymes of resistant Lm and Lactobacillus spp. are more akin to each other (47-63% aa identity) than to that of susceptible La. leichmannii (33-37% aa identity), indicating that the Ddl-related enzymes in these intrinsically resistant species of Gram(+) bacteria exhibit structural differences with those in susceptible species. The Ddl-related enzymes, VanA and VanB, implicated in acquired resistance to glycopeptides in enterococci, were not closely related to their counterparts in Lm and Lactobacillus spp., as they displayed only 26-32% aa identity.

引用

页码：79 / 83

页数：5

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