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Purification and characterization of a high-molecular-weight insecticidal protein complex produced by the entomopathogenic bacterium Photorhabdus luminescens

Article Abstract:

A high-molecular-weight protein complex produced by Photorhabdus luminescens during growth in peptone broth has been isolated and its properties examined. The protein complex has an estimated molecular weight of 1,000,000 and has no protease, phospholipase or hemolytic activity. However, it has been observed to be lethal to a variety of insect larvae. Gel electrophoresis analysis showed that the protein subunits range in size from 30 to 200 kDa.

Author: Bowen, David J., Ensign, Jerald C.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1998
Gram-negative bacteria, Bacterial toxins, Bacterial genetics

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Photobactin: a catechol siderophore produced by Photorhabdus luminescens, an entomopathogen mutually associated with Heterorhabditis bacteriophora NC1 nematodes

Article Abstract:

The authors discuss their study of nematode Heterorhabditis bacteriophora NC1 which transmits Photorhabdus luminescens monoculture to insect hosts. The role of the simbiosis of siderophore and nematode has been investigated via isolation and characterization of a mutant producing no detectable siderophore activity, and the results are reported.

Author: Ensign, Jerald C., Ciche, Todd A., Blackburn, Michael, Carney, John R.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2003
United States, Science & research, Physiological aspects, Environmental aspects, Microbiology, Nematoda, Nematodes, Pathogenic microorganisms, Microbial populations, Catechin, Microbial ecology

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Isolation and characterization of intracellular protein inclusions produced by the entomopathogenic bacterium Photorhabdus luminescens

Article Abstract:

The properties of the two crystalline inclusion proteins from Photorhabdus luminescens are described. They are 11,000 Da but have different amino acid sequences, protease digestion patterns, and immunological cross-reactivities.

Author: Bowen, David J., Ensign, Jerald C.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
Enterobacteriaceae

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Subjects list: Research, Genetic aspects, Bacterial proteins
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