De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis.

Antimicrobial peptides (AMPs), named lycocitin 1, 2 and 3, and a peptide with a monoisotopic molecular mass of 3038.70 Da were detected in the venom glands of the wolf spider Lycosa singoriensis. Two of the peptides, lycocitin 1 and 2, are new AMPs whereas lycocitin 3 is highly homologous to lycotoxin II isolated from the venom of spider Lycosa carolinensis. In addition, two other peptides with monoisotopic masses of 2034.20 and 2340.28 Da showing the motif typical for antimicrobial peptides were also identified. These peptides and lycocitin 1, 2 and 3 were de novo sequenced using electron capture dissociation and low-energy collisional tandem mass spectrometry. The amino acid sequence of lycocitin 1 was determined as GKLQAFLAKMKEIAAQTL-NH(2). Lycocitin 2 differs from lycocitin 1 by a replacement of a lysine residue for an arginine residue at the second position. Lycocitin 3 differs from the known lycotoxin II consisting of 27 amino acid residues by a deletion of Gly-26. Both lycocitin 1 and 2 inhibit growth of Gram-positive (Staphylococcus aureus, Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria and fungi (Candida albicans, Pseudomonas aeruginosa) at micromolar concentrations.

[Molecular cloning and primary structure of cDNA fragment for alpha-latrocrustatoxin from black widow spider venom]. / Molekuliarnoe klonirovanie i opredelenie pervichnoi struktury fragmenta kDNK alpha-latrokrustotoksina iz iada pauka karakurta.

A fragment of the structural gene of alpha-latrocrustotoxin, a new representative of latrotoxins from black widow spider venom, was cloned. The fragment (1191 bp) was obtained by means of PCR based on the data obtained by sequencing tryptic peptides of the toxin. The fragment codes for a 397-aa sequence. The encoded polypeptide is the C-terminal fragment of the toxin central domain that presumably contains a site responsible for the toxin species specificity. The structural similarity of this fragment to the corresponding fragments of other latrotoxins was studied.

[Primary structure of delta-latroinsectotoxin from venom of the Latrodectus mactans tredecimguttatus spider]. / Pervichnaia struktura delta-latroinsektotoksina iz iada pauka Latrodectus mactans tredecimguttatus.

The structural gene of delta-latroinsectotoxin was cloned and its nucleotide sequence was determined. The gene contains an open reading frame of 3642 bp. The deduced amino acid sequence is homologous to the sequences of latrotoxins studied earlier.

[Study of the amino acid sequence of latroinsectotoxin from black widow spider venom]. / Issledovanie aminokislotnoi posledovatel'nosti latroinsektotoksina iz iada pauka karakurta.

The N-terminal amino acid sequence of alpha-latroinsectotoxin from the venom of Latrodectus mactans tredecimguttatus was determined. Then the toxin was digested by trypsin and total or partial amino acid sequences of twenty-six tryptic peptides were established. This resulted in the structural information needed for the construction of probes followed by the cloning of the alpha-latroinsectotoxin structural gene.

[Structure of tryptic fragments of a neurotoxin from black widow spider venom]. / Struktura tripticheskikh fragmentov neirotoksina iz iada pauka karakurta.

The N-terminal amino acid sequence of a neurotoxin from the venom of Latrodectus mactans tredecimguttatus (alpha-latrotoxin) was determined. Latrotoxin was subjected to the tryptic cleavage and total or partial amino acid sequences of 25 peptides were established. In total the tryptic fragments contained 252 amino acid residues. Essential structural information on cloning of the latrotoxin structural gene was obtained.

[Argiopinin-binding proteins from the membrane of the bull cerebral cortex]. / Argiopininsviazyvaiushchii belok iz membran kory mozga byka.

The 40 kDa argiopinin-binding glycoprotein has been isolated from the solubilised preparations of bovine cerebrum membranes by means of two-step biospecific chromatography on affinity sorbents with immobilized glutamate and argiopinins. This receptor component displays a specific L-[3H]glutamate binding with Kd = 0.18 +/- +/- 0.019 mumole and Bmax = 43 +/- 4.5 nmole/mg. Amino acid analysis reveals it to be a member of integral membrane proteins.

[Complete amino acid sequence of neurotoxin Os-1 from the venom of the Central Asian black scorpion Orthochirus scrobiculosus]. / Polnaia aminokislotnaia posledovatel'nost' neirotoksina Os-1 iz iada sredneaziatskogo chernogo skorpiona Orthochirus scrobiculosus.

The neurotoxin Os-1 from the venom of the Central Asian scorpion Orthochirus scrobiculosus possesses a high paralytic activity against mice. This neurotoxin was subjected to tryptic, chymotryptic and BrCN cleavages and its total amino acid sequence was established. It was shown that neurotoxin Os-1 consists of 66 amino acid residues an contains four disulfide bonds.