Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing

Mutation of the zinc-binding metalloprotease motif affects Bacteroides fragilis toxin activity but does not affect propeptide processing
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DOI:
10.1128/iai.73.8.5273-5277.2005
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发表时间:
2005-08-01
影响因子:
3.1
通讯作者:
Sears, CL
Sears, CL
中科院分区:
医学2区
文献类型:
--
作者:
Franco, AA;Buckwold, SL;Sears, CL

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为了评估锌结合金属蛋白酶在脆弱拟杆菌毒素 (BFT) 加工和活性中的作用,通过定点诱变对锌结合共有序列(H348、E349、H352、G355、H358 和 M366)进行突变。我们的结果表明,锌结合金属蛋白酶基序中的单点突变不会影响 BFT 加工,但会降低或消除 BFT 体外生物活性。
To evaluate the role of the zinc-binding metalloprotease in Bacteroides fragilis toxin (BFT) processing and activity, the zinc-binding consensus sequences (H348, E349, H352, G355, H358, and M366) were mutated by site-directed-mutagenesis. Our results indicated that single point mutations in the zinc-binding metalloprotease motif do not affect BFT processing but do reduce or eliminate BFT biologic activity in vitro.