TY - JOUR

T1 - Acipensins - Novel Antimicrobial Peptides from Leukocytes of the Russian Sturgeon Acipenser gueldenstaedtii

AU - Shamova, O.V.

AU - Orlov, D.S.

AU - Balandin, S.V.

AU - Shramova, E.I.

AU - Tsvetkova, E.V.

AU - Panteleev, P.V.

AU - Leonova, Y.F.

AU - Tagaev, A.A.

AU - Kokryakov, V.N.

AU - Ovchinnikova, T.V.

PY - 2014

Y1 - 2014

N2 - Antimicrobial peptides (AMPs) play an important role in the innate defense mechanisms in humans and animals. We have isolated and studied a set of antimicrobial peptides from leukocytes of the Russian sturgeon Acipenser gueldenstaedtii belonging to a subclass of chondrosteans, an ancient group of bony fish. Structural analysis of the isolated peptides, designated as acipensins (Ac), revealed in leukocytes of the Russian sturgeon six novel peptides with molecular masses of 5336.2 Da, 3803.0 Da, 5173.0 Da, 4777.5 Da, 5449.4 Da, and 2740.2 Da, designated as Ac1-Ac6, respectively. Complete primary structures of all the isolated peptides were determined, and the biological activities of three major components Ac1, Ac2, and Ac6 were examined. The peptides Ac1, Ac2, Ac3, Ac4, and Ac5 were found to be the N-terminal acetylated fragments 1-50, 1-35, 1-49, 1-44, and 1-51 of the histone H2A, respectively, while Ac6 was shown to be the 62-85 fragment of the histone H2A. The peptides Ac1 and Ac2 displayed potent antimicrobial activity towards Gram-negative and Gram-positive bacteria (Escherichia coli ML35p, Listeria rnonocytogenes EGD, MRSA ATCC 33591) and the fungus Candida albicans 820, while Ac6 proved effective only against Gram-negative bacteria. The efficacy of Ac 1 and Ac2 towards the fungus and MRSA was reduced upon an increase in the ionic strength of the solution. Ad, Ac2, and Ac6, at concentrations close to their minimum inhibitory concentrations, enhanced the permeability of the E.co/i ML35p outer membrane to the chromogenic marker, but they did not affect appreciably the permeability of the bacterial inner membrane in comparison with a potent pore-forming peptide, protegrin 1. Ad, Ac2, and Ac6 revealed no hemolytic activity against human erythrocytes at concentrations of 1 to 40 mu M and had no cytotoxic effect (1 to 20 mu M) on K-562 and U-937 cells in vitro. Our findings suggest that histone-derived peptides serve as important anti-infective host defense molecules.

AB - Antimicrobial peptides (AMPs) play an important role in the innate defense mechanisms in humans and animals. We have isolated and studied a set of antimicrobial peptides from leukocytes of the Russian sturgeon Acipenser gueldenstaedtii belonging to a subclass of chondrosteans, an ancient group of bony fish. Structural analysis of the isolated peptides, designated as acipensins (Ac), revealed in leukocytes of the Russian sturgeon six novel peptides with molecular masses of 5336.2 Da, 3803.0 Da, 5173.0 Da, 4777.5 Da, 5449.4 Da, and 2740.2 Da, designated as Ac1-Ac6, respectively. Complete primary structures of all the isolated peptides were determined, and the biological activities of three major components Ac1, Ac2, and Ac6 were examined. The peptides Ac1, Ac2, Ac3, Ac4, and Ac5 were found to be the N-terminal acetylated fragments 1-50, 1-35, 1-49, 1-44, and 1-51 of the histone H2A, respectively, while Ac6 was shown to be the 62-85 fragment of the histone H2A. The peptides Ac1 and Ac2 displayed potent antimicrobial activity towards Gram-negative and Gram-positive bacteria (Escherichia coli ML35p, Listeria rnonocytogenes EGD, MRSA ATCC 33591) and the fungus Candida albicans 820, while Ac6 proved effective only against Gram-negative bacteria. The efficacy of Ac 1 and Ac2 towards the fungus and MRSA was reduced upon an increase in the ionic strength of the solution. Ad, Ac2, and Ac6, at concentrations close to their minimum inhibitory concentrations, enhanced the permeability of the E.co/i ML35p outer membrane to the chromogenic marker, but they did not affect appreciably the permeability of the bacterial inner membrane in comparison with a potent pore-forming peptide, protegrin 1. Ad, Ac2, and Ac6 revealed no hemolytic activity against human erythrocytes at concentrations of 1 to 40 mu M and had no cytotoxic effect (1 to 20 mu M) on K-562 and U-937 cells in vitro. Our findings suggest that histone-derived peptides serve as important anti-infective host defense molecules.

KW - innate immunity

KW - antimicrobial peptides

KW - sturgeon leukocytes

KW - histone H2A derivatives

KW - acipensin

KW - POLYACRYLAMIDE-GEL ELECTROPHORESIS

KW - SALMON SALMO-SALAR

KW - HISTONE H1

KW - ONCORHYNCHUS-MYKISS

KW - CATHELICIDIN GENE

KW - WINTER FLOUNDER

KW - RAINBOW-TROUT

KW - BETA-DEFENSIN

KW - PARASIN-I

KW - PROTEINS

M3 - статья

VL - 6

SP - 99

EP - 109

JO - Acta Naturae

JF - Acta Naturae

SN - 2075-8251

IS - 4

ER -