Construction of serralysin-like metalloprotease-defcient mutants of Serratia liquefaciens and their virulence in the silkworm, Bombyx mori

Fusako Kaibara, Kazuhiro Iiyama, Yuuka Chieda, Chisa Yasunaga-Aoki, Susumu Shimizu, Man Lee, Takahiro Kusakabe

研究成果: ジャーナルへの寄稿記事

10 引用 (Scopus)

抄録

Serratia liquefaciens FK01 produces two serralysin-like metalloproteases. One of the genes, ser1, has been cloned before. Another gene, designated as ser2, was cloned in this study. The protein encoded by ser2 was a typical serralysin-like metalloprotease, since a zinc binding motif (HEXXHXUGUXH), glycine-rich repeats (GGXGXD), a Met-turn (SXMXY) and an ABC exporter motif (DXXX) were found in the deduced amino acid sequence. In order to investigate the contribution of these proteases to the virulence in an insect, protease- deficient mutants were created. The mutant strains were inoculated to the silkworm, Bombyx mori. The result of the mortality test suggested that we could not show that deficiency in ser1 and ser2 caused a virulence attenuation in the silkworm under our experimental conditions used in this study. It also suggested that other virulence factors existed in the infection in the silkworm.

元の言語英語
ページ(範囲)55-61
ページ数7
ジャーナルJournal of Biotechnology and Sericology
81
発行部数1
DOI
出版物ステータス出版済み - 1 1 2012

Fingerprint

serralysin
Serratia liquefaciens
Serratia
Bombyx
Metalloproteases
metalloproteinases
Bombyx mori
silkworms
Virulence
Amino acids
virulence
Genes
mutants
proteinases
Zinc
Peptide Hydrolases
Proteins
Virulence Factors
genes
amino acid sequences

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Applied Microbiology and Biotechnology
  • Business, Management and Accounting(all)
  • Agricultural and Biological Sciences(all)
  • Insect Science
  • Industrial and Manufacturing Engineering

これを引用

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abstract = "Serratia liquefaciens FK01 produces two serralysin-like metalloproteases. One of the genes, ser1, has been cloned before. Another gene, designated as ser2, was cloned in this study. The protein encoded by ser2 was a typical serralysin-like metalloprotease, since a zinc binding motif (HEXXHXUGUXH), glycine-rich repeats (GGXGXD), a Met-turn (SXMXY) and an ABC exporter motif (DXXX) were found in the deduced amino acid sequence. In order to investigate the contribution of these proteases to the virulence in an insect, protease- deficient mutants were created. The mutant strains were inoculated to the silkworm, Bombyx mori. The result of the mortality test suggested that we could not show that deficiency in ser1 and ser2 caused a virulence attenuation in the silkworm under our experimental conditions used in this study. It also suggested that other virulence factors existed in the infection in the silkworm.",
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AU - Kaibara, Fusako

AU - Iiyama, Kazuhiro

AU - Chieda, Yuuka

AU - Yasunaga-Aoki, Chisa

AU - Shimizu, Susumu

AU - Lee, Man

AU - Kusakabe, Takahiro

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N2 - Serratia liquefaciens FK01 produces two serralysin-like metalloproteases. One of the genes, ser1, has been cloned before. Another gene, designated as ser2, was cloned in this study. The protein encoded by ser2 was a typical serralysin-like metalloprotease, since a zinc binding motif (HEXXHXUGUXH), glycine-rich repeats (GGXGXD), a Met-turn (SXMXY) and an ABC exporter motif (DXXX) were found in the deduced amino acid sequence. In order to investigate the contribution of these proteases to the virulence in an insect, protease- deficient mutants were created. The mutant strains were inoculated to the silkworm, Bombyx mori. The result of the mortality test suggested that we could not show that deficiency in ser1 and ser2 caused a virulence attenuation in the silkworm under our experimental conditions used in this study. It also suggested that other virulence factors existed in the infection in the silkworm.

AB - Serratia liquefaciens FK01 produces two serralysin-like metalloproteases. One of the genes, ser1, has been cloned before. Another gene, designated as ser2, was cloned in this study. The protein encoded by ser2 was a typical serralysin-like metalloprotease, since a zinc binding motif (HEXXHXUGUXH), glycine-rich repeats (GGXGXD), a Met-turn (SXMXY) and an ABC exporter motif (DXXX) were found in the deduced amino acid sequence. In order to investigate the contribution of these proteases to the virulence in an insect, protease- deficient mutants were created. The mutant strains were inoculated to the silkworm, Bombyx mori. The result of the mortality test suggested that we could not show that deficiency in ser1 and ser2 caused a virulence attenuation in the silkworm under our experimental conditions used in this study. It also suggested that other virulence factors existed in the infection in the silkworm.

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