THE ZINC METALLOPROTEASE OF LISTERIA-MONOCYTOGENES IS REQUIRED FOR MATURATION OF PHOSPHATIDYLCHOLINE PHOSPHOLIPASE-C - DIRECT EVIDENCE OBTAINED BY GENE COMPLEMENTATION

被引：55

作者：

POYART, C ^{[1
]}

ABACHIN, E ^{[1
]}

RAZAFIMANANTSOA, I ^{[1
]}

BERCHE, P ^{[1
]}

机构：

[1] UNIV PARIS 05,MICROBIOL LAB,156 RUE VAUGIRARD,F-75724 PARIS 15,FRANCE

来源：

INFECTION AND IMMUNITY | 1993年 / 61卷 / 04期

关键词：

D O I：

10.1128/IAI.61.4.1576-1580.1993

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

The maturation of the 33-kDa proenzyme to the 29-kDa phosphatidylcholine phospholipase C (PC-PLC) of Listeria monocytogenes requires the production of the zinc metalloprotease encoded by mpl, the proximal gene of the lecithinase operon. We recently described a low-virulence lecithinase-deficient mutant of L. monocytogenes EGD-SmR, designated JL762, generated by a single insertion of transposon Tn1545 in mpl. This mutant failed to produce the 29-kDa PC-PLC, an exoenzyme probably involved in cell-to-cell spreading. The role of the product of the mpl gene in production of PC-PLC was investigated in trans-complementation experiments. The entire mpl gene was cloned in a plasmid able to replicate in L. monocytogenes. This recombinant plasmid was introduced into JL762 and restored the lecithinase phenotype on egg yolk agar and the production of the active 29-kDa PC-PLC in culture supernatants and partially restored the level of virulence. These results demonstrate that zinc-dependent metalloprotease of L. monocytogenes is involved in the virulence of this bacteria at least through its action on PC-PLC.

引用

页码：1576 / 1580

页数：5

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