Determination of the protease cleavage site repertoire--the RNase H but not the RT domain is essential for foamy viral protease activity.
Determination of the protease cleavage site repertoire--the RNase H but not the RT domain is essential for foamy viral protease activity.
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确定蛋白酶裂解位点库 - RNase H 而不是 RT 结构域对于泡沫病毒蛋白酶活性至关重要
DOI:
10.1016/j.virol.2014.02.013
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发表时间:
2014
期刊:
影响因子:
3.7
通讯作者:
J. Bodem
中科院分区:
文献类型:
--
作者:
Spannaus;J. Bodem
In contrast to orthoretroviruses, the foamy virus protease is only active as a protease-reverse transcriptase fusion protein and requires viral RNA for activation. Maturation of foamy viral proteins seems to be restricted to a single cleavage site in Gag and Pol. We provide evidence that unprocessed Gag is required for optimal infectivity, which is unique among retroviruses. Analyses of the cleavage site sequences of the Gag and Pol cleavage sites revealed a high similarity compared to those of Lentiviruses. We show that positions P2׳ and P2 are invariant and that Gag and Pol cleavage sites are processed with similar efficiencies. The RNase H domain is essential for protease activity, but can functionally be substituted by RNase H domains of other retroviruses. Thus, the RNase H domain might be involved in the stabilization of the protease dimer, while the RT domain is essential for RNA dependent protease activation.
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DOI:
--
发表时间:
2011
期刊:
影响因子:
--
作者:
ScienceDirect
通讯作者:
ScienceDirect
影响因子:
5.4
作者:
Huetter, Sylvia;Muellers, Erik;Lindemann, Dirk
通讯作者:
Lindemann, Dirk
DOI:
10.1002/prot.24394
发表时间:
2014
期刊:
Proteins: Structure
影响因子:
--
作者:
Schneider A;Peter D;Schmitt J;Richter F;Rösch P;Wöhrl BM;Hartl MJ
通讯作者:
Hartl MJ
影响因子:
5.4
作者:
Sundquist, Wesley I.;Kraeusslich, Hans-Georg
通讯作者:
Kraeusslich, Hans-Georg
影响因子:
5.9
作者:
A. Rethwilm
通讯作者:
A. Rethwilm