SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom.
BACKGROUND: Kunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of venomous animals. However, no...
| Main Authors: | , , , , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2011-01-01
|
| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3210814?pdf=render |
| _version_ | 1819094586241318912 |
|---|---|
| author | Ruiming Zhao Hui Dai Su Qiu Tian Li Yawen He Yibao Ma Zongyun Chen Yingliang Wu Wenxin Li Zhijian Cao |
| author_facet | Ruiming Zhao Hui Dai Su Qiu Tian Li Yawen He Yibao Ma Zongyun Chen Yingliang Wu Wenxin Li Zhijian Cao |
| author_sort | Ruiming Zhao |
| collection | DOAJ |
| description | BACKGROUND: Kunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of venomous animals. However, no Kunitz-type peptides from scorpion venom have been functionally characterized. PRINCIPAL FINDINGS: A new Kunitz-type venom peptide gene precursor, SdPI, was cloned and characterized from a venom gland cDNA library of the scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of 59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin inhibitory activity with high potency (K(i) = 1.6×10(-7) M) and thermostability. CONCLUSIONS: The results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-type venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived from scorpion venom, and it represents a new class of Kunitz-type venom peptides. |
| first_indexed | 2024-12-21T23:29:45Z |
| format | Article |
| id | doaj.art-60c51e3dbbff445999665926918f98b4 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T23:29:45Z |
| publishDate | 2011-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-60c51e3dbbff445999665926918f98b42022-12-21T18:46:32ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01611e2754810.1371/journal.pone.0027548SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom.Ruiming ZhaoHui DaiSu QiuTian LiYawen HeYibao MaZongyun ChenYingliang WuWenxin LiZhijian CaoBACKGROUND: Kunitz-type venom peptides have been isolated from a wide variety of venomous animals. They usually have protease inhibitory activity or potassium channel blocking activity, which by virtue of the effects on predator animals are essential for the survival of venomous animals. However, no Kunitz-type peptides from scorpion venom have been functionally characterized. PRINCIPAL FINDINGS: A new Kunitz-type venom peptide gene precursor, SdPI, was cloned and characterized from a venom gland cDNA library of the scorpion Lychas mucronatus. It codes for a signal peptide of 21 residues and a mature peptide of 59 residues. The mature SdPI peptide possesses a unique cysteine framework reticulated by three disulfide bridges, different from all reported Kunitz-type proteins. The recombinant SdPI peptide was functionally expressed. It showed trypsin inhibitory activity with high potency (K(i) = 1.6×10(-7) M) and thermostability. CONCLUSIONS: The results illustrated that SdPI is a potent and stable serine protease inhibitor. Further mutagenesis and molecular dynamics simulation revealed that SdPI possesses a serine protease inhibitory active site similar to other Kunitz-type venom peptides. To our knowledge, SdPI is the first functionally characterized Kunitz-type trypsin inhibitor derived from scorpion venom, and it represents a new class of Kunitz-type venom peptides.http://europepmc.org/articles/PMC3210814?pdf=render |
| spellingShingle | Ruiming Zhao Hui Dai Su Qiu Tian Li Yawen He Yibao Ma Zongyun Chen Yingliang Wu Wenxin Li Zhijian Cao SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. PLoS ONE |
| title | SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. |
| title_full | SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. |
| title_fullStr | SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. |
| title_full_unstemmed | SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. |
| title_short | SdPI, the first functionally characterized Kunitz-type trypsin inhibitor from scorpion venom. |
| title_sort | sdpi the first functionally characterized kunitz type trypsin inhibitor from scorpion venom |
| url | http://europepmc.org/articles/PMC3210814?pdf=render |
| work_keys_str_mv | AT ruimingzhao sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT huidai sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT suqiu sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT tianli sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT yawenhe sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT yibaoma sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT zongyunchen sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT yingliangwu sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT wenxinli sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom AT zhijiancao sdpithefirstfunctionallycharacterizedkunitztypetrypsininhibitorfromscorpionvenom |