Essential role of the consensus nucleotide binding site of PtlH in secretion of pertussis toxin from Bordetella pertussis

被引：13

作者：

Kotob, SI ^{[1
]}

Burns, DL ^{[1
]}

机构：

[1] US FDA,CTR BIOL EVALUAT & RES,LAB PERTUSSIS,BETHESDA,MD 20892

来源：

JOURNAL OF BACTERIOLOGY | 1997年 / 179卷 / 23期

关键词：

D O I：

10.1128/jb.179.23.7577-7580.1997

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

PtlH is a member of a specialized set of transport proteins that is essential for secretion of pertussis toxin (PT) from Bordetella pertussis. Previously, PtlH was shown to contain a consensus nucleotide-binding motif. Here, we demonstrate that introduction of plasmids containing mutant forms of ptlH, altered in the putative nucleotide-binding region, into a wild-type strain of B. pertussis resulted in inhibition of PT secretion. Thus, this region of PtlH appears to be essential for protein function. Moreover, the observed dominant negative phenotype suggests that PtlH either functions as a multimer or interacts with another component necessary for secretion of PT.

引用

页码：7577 / 7580

页数：4

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