Bombyx mori cecropin A has a high antifungal activity to entomopathogenic fungus Beauveria bassiana

A cDNA encoding cecropin A (CecA) was cloned from the larvae of silkworm, Bombyx mori, using RT-PCR. It encodes a protein of 63 amino acids, containing a 22 amino acid signal peptide and a 37 amino acid mat peptide of functional domain. The CecA secondary structure contains two typical amphiphilic α...

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Veröffentlicht in:	Gene 2016-05, Vol.583 (1), p.29-35
Hauptverfasser:	Lu, Dingding, Geng, Tao, Hou, Chengxiang, Huang, Yuxia, Qin, Guangxing, Guo, Xijie
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals antifungal activity Antifungal Agents - pharmacology Antimicrobial Cationic Peptides - chemistry Antimicrobial Cationic Peptides - genetics Antimicrobial Cationic Peptides - metabolism Antimicrobial Cationic Peptides - pharmacology Beauveria - drug effects Beauveria - pathogenicity Beauveria bassiana Bombyx - genetics Bombyx - microbiology Bombyx mori cecropin A Cloning, Molecular Gene Expression Regulation Host-Pathogen Interactions - genetics Immunity, Innate - genetics Insect Proteins - genetics Insect Proteins - metabolism Larva - genetics Larva - microbiology Molecular Sequence Data Recombinant Proteins - genetics Recombinant Proteins - pharmacology
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