Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae

Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology
Sung Moon YoeIn Seok Bang

Abstract

Hinnavins, together with lysozymes, are the main types of antibacterial peptides/proteins previously isolated from the larval haemolymph of the cabbage butterfly, Artogeia rapae as part of the humoral immune response to a bacterial invasion. One of these antibacterial peptides, named hinnavin II, was purified and characterized after cDNA cloning. The purified hinnavin II was more active against Gram negative than against Gram positive bacteria. Hinnavin II also showed a powerful synergistic effect on the inhibition of bacterial growth with purified lysozyme. The cDNA has a total length of 186 bp with a 114 coding region. The deduced protein sequence contains 38 amino acids with a coding capacity of 4142.8 Da. The result of a multiple sequence alignment and phylogenetic analysis with Clustal W indicated that mature hinnavin II showed an approximately 78.9% amino acid sequence identity with cecropin A and originated from a group containing mostly lepidopteran cecropins.

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Citations

May 26, 2010·Applied Microbiology and Biotechnology·Xue-mei LuXiao-bo Li
May 23, 2012·International Journal of Peptides·C PolancoJ A Castanon-Gonzalez
May 9, 2014·Applied Microbiology and Biotechnology·Hui-Yu YiXiao-Qiang Yu
Feb 13, 2014·The Journal of Antibiotics·Nidhi Singh, Jayanthi Abraham
Jun 21, 2014·Developmental and Comparative Immunology·Anchalee TassanakajonPiti Amparyup
Sep 29, 2007·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Li WangYi Pang
Dec 1, 1999·Developmental and Comparative Immunology·A E Halwani, G B Dunphy
Nov 27, 2019·International Journal of Molecular Sciences·Daniel BradyFederica Sandrelli

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