A lysine rich C-terminal tail is directly involved in the toxicity of CSTX-1, a neurotoxic peptide from the venom of the spider Cupiennius salei

Autor:	L, Kuhn-Nentwig, J, Schaller, U, Kämpfer, H, Imboden, H, Malli, W, Nentwig
Rok vydání:	2000
Předmět:	Binding Sites Lysine Molecular Sequence Data Neurotoxins Spider Venoms Spiders Reptilian Proteins Enteropeptidase Drosophila melanogaster Endopeptidases Factor Xa Animals Biological Assay Amino Acid Sequence Amino Acids Peptides Sequence Analysis
Zdroj:	Archives of insect biochemistry and physiology. 44(3)
ISSN:	0739-4462
Popis:	CSTX-1 (74 amino acids, 8,352.62 Da) is a potent neurotoxin from the venom of Cupiennius salei. With the monoclonal antibody 9H3 against CSTX-1, we identified two similar peptides by Western blot analysis. These two peptides were purified by RP-HPLC: CSTX-2a (61 amino acids, 6865.75 Da) and CSTX-2b (60 amino acids, 6709.57 Da). Using ESI-MS analysis and sequencing we verified that CSTX-2a is a truncated version of CSTX-1. CSTX-2b differs from CSTX-2a by the absence of Arg61. Toxicity of CSTX-1, CSTX-2a, and CSTX-2b to Drosophila melanogaster showed that the absence of the last 13 amino acids of CSTX-1 results in a seven-fold activity loss. CSTX-2b, which lacks Arg61 is 190-fold less toxic. We conclude that the C-terminal part of CSTX-1, especially Arg61, is essential for the expression of toxicity. CSTX-1 is degraded to CSTX-2a and CSTX-2b by proteases that are released from venom gland cells by apocrine secretion.
Databáze:	OpenAIRE
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