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

Sung Moon Yoe, Chang Soo Kang, Sung Sik Han, In Seok Bang

Research output: Contribution to journalArticle

17 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)199-205
Number of pages7
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume144
Issue number2
DOIs
Publication statusPublished - 2006 Jun 1

Fingerprint

Cecropins
Butterflies
Cloning
Brassica
Muramidase
Organism Cloning
Complementary DNA
Amino Acids
Peptides
Hemolymph
Sequence Alignment
Gram-Positive Bacteria
Humoral Immunity
Amino Acid Sequence
Bacteria
Proteins
Growth

Keywords

  • 5′-rapid amplification of cDNA ends (RACE)
  • Antibacterial peptide
  • Artogeia rapae
  • Cecropin
  • Hinnavin II
  • Hinnavin II gene
  • Insect immunity
  • MALDI-MS

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

Cite this

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title = "Characterization and cDNA cloning of hinnavin II, a cecropin family antibacterial peptide from the cabbage butterfly, Artogeia rapae",
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.",
keywords = "5′-rapid amplification of cDNA ends (RACE), Antibacterial peptide, Artogeia rapae, Cecropin, Hinnavin II, Hinnavin II gene, Insect immunity, MALDI-MS",
author = "Yoe, {Sung Moon} and Kang, {Chang Soo} and Han, {Sung Sik} and Bang, {In Seok}",
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AU - Yoe, Sung Moon

AU - Kang, Chang Soo

AU - Han, Sung Sik

AU - Bang, In Seok

PY - 2006/6/1

Y1 - 2006/6/1

N2 - 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.

AB - 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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KW - Insect immunity

KW - MALDI-MS

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