Functional expression of α-latrotoxin in baculovirus system

Kirill E. Volynski, Elena D. Nosyreva, Yuri A. Ushkaryov, Eugene V. Grishin

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


To facilitate the study of the mechanism of α-latrotoxin action, it is necessary to create a biologically active recombinant toxin. Mature α-latrotoxin is naturally produced by post-translational cleavage, probably at two furin sites located at the N- and C-termini of the precursor. A recombinant baculovirus has now been constructed, which encodes the melittin signal peptide fused to the 130-kDa mature toxin between the furin sites. Insect cells, infected with this baculovirus, secreted recombinant α-latrotoxin. This was partially purified and proved indistinguishable from the natural toxin with respect to its molecular mass, immunostaining, toxicity to mice, binding to α-latrotoxin receptors (latrophilin or neurexin Iα) and electrophysiological recording in the mouse diaphragm. The successful expression of recombinant α-latrotoxin permits mutational analysis of the toxin. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)25-28
Number of pages4
JournalFEBS Letters
Issue number1
StatePublished - Jan 8 1999


  • Baculovirus
  • Expression
  • Latrophilin
  • Neurexin
  • α-Latrotoxin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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