Limits...
Pathogenicity of Isolates of Serratia Marcescens towards Larvae of the Scarab Phyllophaga Blanchardi (Coleoptera).

Pineda-Castellanos ML, Rodríguez-Segura Z, Villalobos FJ, Hernández L, Lina L, Nuñez-Valdez ME - Pathogens (2015)

Bottom Line: Oral and injection bioassays using healthy Phyllophaga blanchardi larvae fed with the S. marcescens isolates showed different degrees of antifeeding effect and mortality.S. marcescens (Sm81) cell-free culture supernatant caused significant antifeeding effect and mortality to P. blanchardi larvae by oral bioassay and also mortality by injection bioassay.This insecticidal protein could have applications in agricultural biotechnology.

View Article: PubMed Central - PubMed

Affiliation: Centro de Investigación en Dinámica Celular, Instituto de Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, CP 62209, Cuernavaca, Morelos, Mexico. mlpc@uaem.mx.

ABSTRACT
Serratia marcescens is a Gram negative bacterium (Enterobacteriaceae) often associated with infection of insects. In order to find pathogenic bacteria with the potential to control scarab larvae, several bacterial strains were isolated from the hemocoel of diseased Phyllophaga spp (Coleoptera:Scarabaeidae) larvae collected from cornfields in Mexico. Five isolates were identified as Serratia marcescens by 16S rRNA gene sequencing and biochemical tests. Oral and injection bioassays using healthy Phyllophaga blanchardi larvae fed with the S. marcescens isolates showed different degrees of antifeeding effect and mortality. No insecticidal activity was observed for Spodoptera frugiperda larvae (Lepidoptera: Noctuidae) by oral inoculation. S. marcescens (Sm81) cell-free culture supernatant caused significant antifeeding effect and mortality to P. blanchardi larvae by oral bioassay and also mortality by injection bioassay. Heat treated culture broths lost the ability to cause disease symptoms, suggesting the involvement of proteins in the toxic activity. A protein of 50.2 kDa was purified from the cell-free broth and showed insecticidal activity by injection bioassay towards P. blanchardi. Analysis of the insecticidal protein by tandem- mass spectrometry (LC-MS/MS) showed similarity to a Serralysin-like protein from S. marcescens spp. This insecticidal protein could have applications in agricultural biotechnology.

No MeSH data available.


Related in: MedlinePlus

Amino acid sequence of the Serralysin protein (Accession V9NCZ4) showing homology to 22 peptides from Sm81P50. Amino acids shaded in green represent identical peptides that were identified by mass spectrometry. Amino acids shaded in yellow represent peptides also identified by mass spectrometry but not identical to the V9NCZ4 Serralysin.
© Copyright Policy
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4493471&req=5

pathogens-04-00210-f007: Amino acid sequence of the Serralysin protein (Accession V9NCZ4) showing homology to 22 peptides from Sm81P50. Amino acids shaded in green represent identical peptides that were identified by mass spectrometry. Amino acids shaded in yellow represent peptides also identified by mass spectrometry but not identical to the V9NCZ4 Serralysin.

Mentions: Analysis of the insecticidal protein by tandem- mass spectrometry (LC-MS/MS) showed a similarity to a Serralysin-like protein from the Serratia spp protein group accession A8G880; [12]. Analysis of the tryptic digest of Sm81P50 identified 22 peptides that covered 65.2% of the homolog protein Serralysin (Accession V9NCZ4), with a molecular weight of 50.2 kDa, including peptides from the central region of the protein and the C termini (Figure 7).


Pathogenicity of Isolates of Serratia Marcescens towards Larvae of the Scarab Phyllophaga Blanchardi (Coleoptera).

Pineda-Castellanos ML, Rodríguez-Segura Z, Villalobos FJ, Hernández L, Lina L, Nuñez-Valdez ME - Pathogens (2015)

Amino acid sequence of the Serralysin protein (Accession V9NCZ4) showing homology to 22 peptides from Sm81P50. Amino acids shaded in green represent identical peptides that were identified by mass spectrometry. Amino acids shaded in yellow represent peptides also identified by mass spectrometry but not identical to the V9NCZ4 Serralysin.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4493471&req=5

pathogens-04-00210-f007: Amino acid sequence of the Serralysin protein (Accession V9NCZ4) showing homology to 22 peptides from Sm81P50. Amino acids shaded in green represent identical peptides that were identified by mass spectrometry. Amino acids shaded in yellow represent peptides also identified by mass spectrometry but not identical to the V9NCZ4 Serralysin.
Mentions: Analysis of the insecticidal protein by tandem- mass spectrometry (LC-MS/MS) showed a similarity to a Serralysin-like protein from the Serratia spp protein group accession A8G880; [12]. Analysis of the tryptic digest of Sm81P50 identified 22 peptides that covered 65.2% of the homolog protein Serralysin (Accession V9NCZ4), with a molecular weight of 50.2 kDa, including peptides from the central region of the protein and the C termini (Figure 7).

Bottom Line: Oral and injection bioassays using healthy Phyllophaga blanchardi larvae fed with the S. marcescens isolates showed different degrees of antifeeding effect and mortality.S. marcescens (Sm81) cell-free culture supernatant caused significant antifeeding effect and mortality to P. blanchardi larvae by oral bioassay and also mortality by injection bioassay.This insecticidal protein could have applications in agricultural biotechnology.

View Article: PubMed Central - PubMed

Affiliation: Centro de Investigación en Dinámica Celular, Instituto de Ciencias Básicas y Aplicadas, Universidad Autónoma del Estado de Morelos, Av. Universidad 1001, Col. Chamilpa, CP 62209, Cuernavaca, Morelos, Mexico. mlpc@uaem.mx.

ABSTRACT
Serratia marcescens is a Gram negative bacterium (Enterobacteriaceae) often associated with infection of insects. In order to find pathogenic bacteria with the potential to control scarab larvae, several bacterial strains were isolated from the hemocoel of diseased Phyllophaga spp (Coleoptera:Scarabaeidae) larvae collected from cornfields in Mexico. Five isolates were identified as Serratia marcescens by 16S rRNA gene sequencing and biochemical tests. Oral and injection bioassays using healthy Phyllophaga blanchardi larvae fed with the S. marcescens isolates showed different degrees of antifeeding effect and mortality. No insecticidal activity was observed for Spodoptera frugiperda larvae (Lepidoptera: Noctuidae) by oral inoculation. S. marcescens (Sm81) cell-free culture supernatant caused significant antifeeding effect and mortality to P. blanchardi larvae by oral bioassay and also mortality by injection bioassay. Heat treated culture broths lost the ability to cause disease symptoms, suggesting the involvement of proteins in the toxic activity. A protein of 50.2 kDa was purified from the cell-free broth and showed insecticidal activity by injection bioassay towards P. blanchardi. Analysis of the insecticidal protein by tandem- mass spectrometry (LC-MS/MS) showed similarity to a Serralysin-like protein from S. marcescens spp. This insecticidal protein could have applications in agricultural biotechnology.

No MeSH data available.


Related in: MedlinePlus