Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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.
в: Biochemistry (Moscow), Том 71, № 8, 01.08.2006, стр. 879-883.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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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