Standard

α-Defensins from blood leukocytes of the monkey Papio hamadryas. / Tsvetkova, E. V.; Aleshina, G. M.; Shamova, O. V.; Leonova, L. E.; Lehrer, R. I.; Kokryakov, V. N.

In: Biochemistry (Moscow), Vol. 71, No. 8, 01.08.2006, p. 879-883.

Research output: Contribution to journalArticlepeer-review

Harvard

APA

Vancouver

Author

Tsvetkova, E. V. ; Aleshina, G. M. ; Shamova, O. V. ; Leonova, L. E. ; Lehrer, R. I. ; Kokryakov, V. N. / α-Defensins from blood leukocytes of the monkey Papio hamadryas. In: Biochemistry (Moscow). 2006 ; Vol. 71, No. 8. pp. 879-883.

BibTeX

@article{c84753845825466c94c755d46efc36d1,
title = "α-Defensins from blood leukocytes of the monkey Papio hamadryas",
abstract = "Three antimicrobial peptides named PHD1-3 (Papio hamadryas defensin) have been isolated from hamadryas baboon blood leukocytes using preparative electrophoresis and reverse-phase HPLC. The primary structures of these peptides have been determined by automated Edman degradation and mass-spectrometry. The results suggest that the peptides belong to the α-defensin family. Structural homology analysis reveals that among α-defensins from other animal species, PHD3 is the most closely related to RMAD5 (rhesus macaque α-defensin) (90% homology) from rhesus macaque leukocytes and also highly similar to human α-defensin HD5 (60% homology), which is produced by intestinal Paneth cells. The homology of PHD3 with human neutrophil α-defensin HNP1 (human natural peptide) was 30%. The primary structures of PHD1 and PHD2 are most similar to RED1 (rhesus enteral defensin), one of six enteral α-defensins of rhesus monkeys. PHD1-3 have been shown to be active against the Gram-positive bacteria Listeria monocytogenes and Staphylococcus aureus, the Gram-negative bacterium Escherichia coli, and the fungus Candida albicans, similarly to the human HNP1 defensin.",
keywords = "α-defensins, Antimicrobial peptides of mammals, Leukocytes, Monkey, Papio hamadryas, Primary structure",
author = "Tsvetkova, {E. V.} and Aleshina, {G. M.} and Shamova, {O. V.} and Leonova, {L. E.} and Lehrer, {R. I.} and Kokryakov, {V. N.}",
year = "2006",
month = aug,
day = "1",
doi = "10.1134/S0006297906080098",
language = "English",
volume = "71",
pages = "879--883",
journal = "Biochemistry (Moscow)",
issn = "0006-2979",
publisher = "МАИК {"}Наука/Интерпериодика{"}",
number = "8",

}

RIS

TY - JOUR

T1 - α-Defensins from blood leukocytes of the monkey Papio hamadryas

AU - Tsvetkova, E. V.

AU - Aleshina, G. M.

AU - Shamova, O. V.

AU - Leonova, L. E.

AU - Lehrer, R. I.

AU - Kokryakov, V. N.

PY - 2006/8/1

Y1 - 2006/8/1

N2 - Three antimicrobial peptides named PHD1-3 (Papio hamadryas defensin) have been isolated from hamadryas baboon blood leukocytes using preparative electrophoresis and reverse-phase HPLC. The primary structures of these peptides have been determined by automated Edman degradation and mass-spectrometry. The results suggest that the peptides belong to the α-defensin family. Structural homology analysis reveals that among α-defensins from other animal species, PHD3 is the most closely related to RMAD5 (rhesus macaque α-defensin) (90% homology) from rhesus macaque leukocytes and also highly similar to human α-defensin HD5 (60% homology), which is produced by intestinal Paneth cells. The homology of PHD3 with human neutrophil α-defensin HNP1 (human natural peptide) was 30%. The primary structures of PHD1 and PHD2 are most similar to RED1 (rhesus enteral defensin), one of six enteral α-defensins of rhesus monkeys. PHD1-3 have been shown to be active against the Gram-positive bacteria Listeria monocytogenes and Staphylococcus aureus, the Gram-negative bacterium Escherichia coli, and the fungus Candida albicans, similarly to the human HNP1 defensin.

AB - Three antimicrobial peptides named PHD1-3 (Papio hamadryas defensin) have been isolated from hamadryas baboon blood leukocytes using preparative electrophoresis and reverse-phase HPLC. The primary structures of these peptides have been determined by automated Edman degradation and mass-spectrometry. The results suggest that the peptides belong to the α-defensin family. Structural homology analysis reveals that among α-defensins from other animal species, PHD3 is the most closely related to RMAD5 (rhesus macaque α-defensin) (90% homology) from rhesus macaque leukocytes and also highly similar to human α-defensin HD5 (60% homology), which is produced by intestinal Paneth cells. The homology of PHD3 with human neutrophil α-defensin HNP1 (human natural peptide) was 30%. The primary structures of PHD1 and PHD2 are most similar to RED1 (rhesus enteral defensin), one of six enteral α-defensins of rhesus monkeys. PHD1-3 have been shown to be active against the Gram-positive bacteria Listeria monocytogenes and Staphylococcus aureus, the Gram-negative bacterium Escherichia coli, and the fungus Candida albicans, similarly to the human HNP1 defensin.

KW - α-defensins

KW - Antimicrobial peptides of mammals

KW - Leukocytes

KW - Monkey

KW - Papio hamadryas

KW - Primary structure

UR - http://www.scopus.com/inward/record.url?scp=33747690989&partnerID=8YFLogxK

U2 - 10.1134/S0006297906080098

DO - 10.1134/S0006297906080098

M3 - Article

C2 - 16978151

AN - SCOPUS:33747690989

VL - 71

SP - 879

EP - 883

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 8

ER -

ID: 48956466