Tags

Type your tag names separated by a space and hit enter

An insecticidal protein from Xenorhabdus budapestensis that results in prophenoloxidase activation in the wax moth, Galleria mellonella.
J Invertebr Pathol. 2012 May; 110(1):60-7.JI

Abstract

Xenorhabdus budapestensis can produce a variety of proteins that help this bacterium and its mutualistic nematode vector kill the host insect. In this report, we purified one protein fraction from the intracellular extract of X. budapestensis D43, which was designated HIP57. By injection, HIP57 caused Galleria mellonella larval bodies to blacken and die with an LD(50) of 206.81 ng/larva. Analyzes of HIP57 by two-dimensional gel electrophoresis showed that this protein was a single spot on the gel with a molecular weight of 57 kDa and a pI of ∼5. Sequencing and bioinformatic analysis suggested that the HIP57 toxin was homologous to GroEL. GroEL has been accepted as molecule chaperon; however, our research revealed that HIP57 (GroEL) possesses another novel function as an insecticide. A GroEL phylogenetic tree defined the relationship among the related species of mutualistic bacteria (Xenorhabdus and Photorhabdus) from the entomopathogenic nematodes and the evolution within the family Enterobacteriaceae. Thus, GroEL could be a complement to 16S rDNA for studying the molecular phylogenies of the family Enterobacteriaceae. Phenoloxidase (PO) activity analysis of G. mellonella larvae injected with HIP57 suggested that the toxin activates the PO cascade, which provides an extensive defense reaction that potentially responsible for G. mellonella larval death.

Authors+Show Affiliations

College of Plant Protection, Anhui Agricultural University, Hefei 230036, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22387345

Citation

Yang, Jun, et al. "An Insecticidal Protein From Xenorhabdus Budapestensis That Results in Prophenoloxidase Activation in the Wax Moth, Galleria Mellonella." Journal of Invertebrate Pathology, vol. 110, no. 1, 2012, pp. 60-7.
Yang J, Zeng HM, Lin HF, et al. An insecticidal protein from Xenorhabdus budapestensis that results in prophenoloxidase activation in the wax moth, Galleria mellonella. J Invertebr Pathol. 2012;110(1):60-7.
Yang, J., Zeng, H. M., Lin, H. F., Yang, X. F., Liu, Z., Guo, L. H., Yuan, J. J., & Qiu, D. W. (2012). An insecticidal protein from Xenorhabdus budapestensis that results in prophenoloxidase activation in the wax moth, Galleria mellonella. Journal of Invertebrate Pathology, 110(1), 60-7. https://doi.org/10.1016/j.jip.2012.02.006
Yang J, et al. An Insecticidal Protein From Xenorhabdus Budapestensis That Results in Prophenoloxidase Activation in the Wax Moth, Galleria Mellonella. J Invertebr Pathol. 2012;110(1):60-7. PubMed PMID: 22387345.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - An insecticidal protein from Xenorhabdus budapestensis that results in prophenoloxidase activation in the wax moth, Galleria mellonella. AU - Yang,Jun, AU - Zeng,Hong-Mei, AU - Lin,Hua-Feng, AU - Yang,Xiu-Fen, AU - Liu,Zheng, AU - Guo,Li-Hua, AU - Yuan,Jing-Jing, AU - Qiu,De-Wen, Y1 - 2012/02/23/ PY - 2011/12/13/received PY - 2012/02/08/revised PY - 2012/02/10/accepted PY - 2012/3/6/entrez PY - 2012/3/6/pubmed PY - 2012/8/9/medline SP - 60 EP - 7 JF - Journal of invertebrate pathology JO - J Invertebr Pathol VL - 110 IS - 1 N2 - Xenorhabdus budapestensis can produce a variety of proteins that help this bacterium and its mutualistic nematode vector kill the host insect. In this report, we purified one protein fraction from the intracellular extract of X. budapestensis D43, which was designated HIP57. By injection, HIP57 caused Galleria mellonella larval bodies to blacken and die with an LD(50) of 206.81 ng/larva. Analyzes of HIP57 by two-dimensional gel electrophoresis showed that this protein was a single spot on the gel with a molecular weight of 57 kDa and a pI of ∼5. Sequencing and bioinformatic analysis suggested that the HIP57 toxin was homologous to GroEL. GroEL has been accepted as molecule chaperon; however, our research revealed that HIP57 (GroEL) possesses another novel function as an insecticide. A GroEL phylogenetic tree defined the relationship among the related species of mutualistic bacteria (Xenorhabdus and Photorhabdus) from the entomopathogenic nematodes and the evolution within the family Enterobacteriaceae. Thus, GroEL could be a complement to 16S rDNA for studying the molecular phylogenies of the family Enterobacteriaceae. Phenoloxidase (PO) activity analysis of G. mellonella larvae injected with HIP57 suggested that the toxin activates the PO cascade, which provides an extensive defense reaction that potentially responsible for G. mellonella larval death. SN - 1096-0805 UR - https://www.unboundmedicine.com/medline/citation/22387345/An_insecticidal_protein_from_Xenorhabdus_budapestensis_that_results_in_prophenoloxidase_activation_in_the_wax_moth_Galleria_mellonella_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2011(12)00035-3 DB - PRIME DP - Unbound Medicine ER -