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Title of Journal: Appl Biochem Biotechnol

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Abbravation: Applied Biochemistry and Biotechnology

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Springer-Verlag

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DOI

10.1016/0040-1951(91)90379-7

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1559-0291

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Identification of New DominantNegative Mutants of

Authors: Gaobing Wu Chunfang Feng Sha Cao Aizhen Guo Ziduo Liu
Publish Date: 2012/09/05
Volume: 168, Issue: 5, Pages: 1302-1310
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Abstract

The anthrax toxin is composed of three proteins protective antigen PA lethal factor LF and edema toxin EF The PA moiety carries EF and LF into the cytosol of mammalian cells via a mechanism that depends on the oligomerization of PA and transmembrane pore formation by the PA oligomer Certain mutants of PA termed dominantnegative DN mutants can cooligomerize with wildtype PA and disrupt the translocation ability of the pore Here we constructed a PA mutant library by introducing random mutations into domain II of PA and screened three new DN mutants of PA V377E T380S and I432C All the mutants inhibited the anthrax toxin action against sensitive cells V377E had the strongest inhibitory effect and was further confirmed to be able to protect mice against a challenge with anthrax lethal toxin Furthermore we functionally characterized these mutants The result showed that these mutations did not impair proteolytic activation or oligomer formation of PA but impeded the prepore–pore conversion of the oligomer These DN mutants of PA identified in our study may provide valuable information for elucidating the structure–function relationship of PA and for designing therapeutics for anthrax treatment

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