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

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Standard

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.

I: Journal of Mass Spectrometry, Bind 39, Nr. 2, 2004, s. 193-201.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Budnik, BA, Olsen, JV, Egorov, TA, Anisimova, VE, Galkina, TG, Musolyamov, AK, Grishin, EV & Zubarev, RA 2004, 'De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis', Journal of Mass Spectrometry, bind 39, nr. 2, s. 193-201. https://doi.org/10.1002/jms.577

APA

Budnik, B. A., Olsen, J. V., Egorov, T. A., Anisimova, V. E., Galkina, T. G., Musolyamov, A. K., Grishin, E. V., & Zubarev, R. A. (2004). De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. Journal of Mass Spectrometry, 39(2), 193-201. https://doi.org/10.1002/jms.577

Vancouver

Budnik BA, Olsen JV, Egorov TA, Anisimova VE, Galkina TG, Musolyamov AK o.a. De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. Journal of Mass Spectrometry. 2004;39(2):193-201. https://doi.org/10.1002/jms.577

Author

Budnik, B A ; Olsen, Jesper Velgaard ; Egorov, T A ; Anisimova, V E ; Galkina, T G ; Musolyamov, A K ; Grishin, E V ; Zubarev, R A. / De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis. I: Journal of Mass Spectrometry. 2004 ; Bind 39, Nr. 2. s. 193-201.

Bibtex

@article{c7b9a3d0457011df928f000ea68e967b,
title = "De novo sequencing of antimicrobial peptides isolated from the venom glands of the wolf spider Lycosa singoriensis",
abstract = "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.",
author = "Budnik, {B A} and Olsen, {Jesper Velgaard} and Egorov, {T A} and Anisimova, {V E} and Galkina, {T G} and Musolyamov, {A K} and Grishin, {E V} and Zubarev, {R A}",
note = "Keywords: Amino Acid Sequence; Animals; Anti-Bacterial Agents; Exocrine Glands; Molecular Sequence Data; Peptides; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spider Venoms",
year = "2004",
doi = "10.1002/jms.577",
language = "English",
volume = "39",
pages = "193--201",
journal = "Journal of Mass Spectrometry",
issn = "1076-5174",
publisher = "JohnWiley & Sons Ltd",
number = "2",

}

RIS

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