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Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao

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AbstractChinese tarantula, Chilobrachys jingzhao is one of the most venomous spiders in southern China and its venom is a mixture of various compounds with diversified biological activities. The proteome of C. jingzhao venom was analyzed by proteomic techniques. Proteins with molecular weight of over 10 kDa, indicated by gel‐filtration and SDS‐PAGE, were analyzed using 2‐DE and MALDI‐TOF/TOF and LC/ESI‐Q‐TOF MS. More than 90 proteins were detected, with 47 confirmed by sequence similarity search using mass spectrum driven basic local alignment search tool (MS BLAST). On the other hand, peptides with MW lower than 10 kDa were separated by HPLC and identified by MALDI‐TOF MS and Edman degradation sequencing. About 120 peptides were detected, 60 of which were fully or partially sequenced. Our results indicate that peptides with MW lower than 10 kDa are the major components in the crude venom of C. jingzhao. Like those of other tarantulas, these peptides are very likely to act on various ion channels. These results pave a way for further detailed structure–function correlation analysis of the individual toxins present in the venom of C. jingzhao.
Title: Proteomic and peptidomic analysis of the venom from Chinese tarantula Chilobrachys jingzhao
Description:
AbstractChinese tarantula, Chilobrachys jingzhao is one of the most venomous spiders in southern China and its venom is a mixture of various compounds with diversified biological activities.
The proteome of C.
jingzhao venom was analyzed by proteomic techniques.
Proteins with molecular weight of over 10 kDa, indicated by gel‐filtration and SDS‐PAGE, were analyzed using 2‐DE and MALDI‐TOF/TOF and LC/ESI‐Q‐TOF MS.
More than 90 proteins were detected, with 47 confirmed by sequence similarity search using mass spectrum driven basic local alignment search tool (MS BLAST).
On the other hand, peptides with MW lower than 10 kDa were separated by HPLC and identified by MALDI‐TOF MS and Edman degradation sequencing.
About 120 peptides were detected, 60 of which were fully or partially sequenced.
Our results indicate that peptides with MW lower than 10 kDa are the major components in the crude venom of C.
jingzhao.
Like those of other tarantulas, these peptides are very likely to act on various ion channels.
These results pave a way for further detailed structure–function correlation analysis of the individual toxins present in the venom of C.
jingzhao.

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