Antimicrobial peptide from leukocytes of <em>Vulpes vulpes</em> red fox

Elena Ilina; Mikhail Berlov; Yaroslav Dubrovsky; Elena Bogomolova; Vladimir Kokryakov

Authors

Elena Ilina Saint Petersburg State University, 7–9, Universitetskaya nab., Saint Petersburg, 199034, Russian Federation
Mikhail Berlov Saint Petersburg State University, 7–9, Universitetskaya nab., Saint Petersburg, 199034, Russian Federation; Institute of Experimental Medicine of the North West Branch of the Russian Academy of Medical Sciences, Saint Petersburg, 197376, Russian Federation https://orcid.org/0000-0001-5191-0467
Yaroslav Dubrovsky Institute of Analytical Instrumentation of the Russian Academy of Sciences, Russian Federation
Elena Bogomolova Saint Petersburg State University, 7–9, Universitetskaya nab., Saint Petersburg, 199034, Russian Federation https://orcid.org/0000-0003-4047-4086
Vladimir Kokryakov Institute of Experimental Medicine of the North West Branch of the Russian Academy of Medical Sciences, Saint Petersburg, 197376, Russian Federation; Saint Petersburg State University, 7–9, Universitetskaya nab., Saint Petersburg, 199034, Russian Federation

Abstract

Antimicrobial peptides from animal leukocytes are considered as a possible source of novel medicines additional to conventional antibiotics. Characterization of new antimicrobial peptides from previously unstudied species is important for progress in this direction. The aim of this work was to investigate antimicrobial peptides from red fox leukocytes. Highly purified 4690 D peptide was isolated by the procedure including acetic acid extraction of cationic compounds from leukocytes, gel filtration on Biogel P-10, and reversed phase HPLC on C18. Peptide expressed marked antimicrobial activity to gram-negative bacterium Escherichia coli ML-35p and gram-positive bacterium Listeria monocytogenes EGD. The primary structure of peptide was determined by mass spectrometry of tryptic cleavage products with consecutive analysis of the data by MASCOT service. This peptide was revealed to be a fragment of histone H4 presumably corresponding to 19–59 piece in its amino acid sequence.