De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis
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De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. / Budnik, B A; Olsen, Jesper Velgaard; Egorov, T A; Anisimova, V E; Galkina, T G; Musolyamov, A K; Grishin, E V; Zubarev, R A.
In: Journal of Mass Spectrometry, Vol. 39, No. 2, 2004, p. 193-201.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis
AU - Budnik, B A
AU - Olsen, Jesper Velgaard
AU - Egorov, T A
AU - Anisimova, V E
AU - Galkina, T G
AU - Musolyamov, A K
AU - Grishin, E V
AU - Zubarev, R A
N1 - Keywords: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Exocrine Glands; Molecular Sequence Data; Peptides; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spider Venoms
PY - 2004
Y1 - 2004
N2 - 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.
AB - 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.
U2 - 10.1002/jms.577
DO - 10.1002/jms.577
M3 - Journal article
C2 - 14991689
VL - 39
SP - 193
EP - 201
JO - Journal of Mass Spectrometry
JF - Journal of Mass Spectrometry
SN - 1076-5174
IS - 2
ER -
ID: 19160409