Insecticidal activity of a bacterial crystal protein expressed by a recombinant baculovirus in insect cells.

Appl Environ Microbiol

Department of Virology, Agricultural University Wageningen, P.O. Box 8045, 6700 EM Wageningen, and Center for Plant Breeding Research, P.O. Box 16, 6700 AA Wageningen, The Netherlands.

Published: September 1990

Baculoviruses are insect pathogens with a relatively slow speed of action, and this has limited their use as control agents of insect pests. Introduction into baculoviruses of genes which code for proteins interfering specifically with insect metabolism or metamorphosis, such as toxins, hormones, and enzymes, may enhance the pathogenicity of these viruses. The complete insecticidal crystal protein gene cryIA(b) of Bacillus thuringiensis subsp. aizawai 7.21 was engineered into the nuclear polyhedrosis virus of Autographa californica (AcNPV) in place of the polyhedrin gene. In infected Spodoptera frugiperda cells, the cryIA(b) gene was expressed at a high level without interference with AcNPV production. The crystal protein was found in the cytoplasm of S. frugiperda cells, mainly as large crystals with an ultrastructure similar to that of B. thuringiensis crystals. Infected-cell extracts inhibited feeding of the large cabbage white Pieris brassicae. The toxicity of the crystal protein expressed by AcNPV recombinants was comparable with that of the crystal protein expressed by a corresponding Escherichia coli recombinant.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC184840PMC
http://dx.doi.org/10.1128/aem.56.9.2764-2770.1990DOI Listing

Publication Analysis

Top Keywords

crystal protein
20
protein expressed
12
frugiperda cells
8
crystal
5
protein
5
insecticidal activity
4
activity bacterial
4
bacterial crystal
4
expressed
4
expressed recombinant
4

Similar Publications

A simple and effective method to remove pigments from heterologous secretory proteins expressed in Pichia pastoris.

Adv Biotechnol (Singap)

February 2024

CAS Center for Excellence in Molecular Cell Science, Shanghai Institute of Biochemistry and Cell Biology, University of Chinese Academy of Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai, 200030, China.

Pichia pastoris is a popular yeast host for high-level heterologous expression of proteins on an industrial scale owing to its reliable expression, robust growth, high fermentation density, and easy genetic manipulation and cultivation at a relatively low cost. Of particular interest is its high secretion efficiency for small proteins including insulin, human serum albumin, vaccines, enzymes, and llama-derived heavy-chain only antibodies (nanobodies) for pharmaceutical and research applications. However, a recurring challenge in using P.

View Article and Find Full Text PDF

ISB 1442 is a bispecific biparatopic antibody in clinical development to treat hematological malignancies. It consists of two adjacent anti-CD38 arms targeting non-overlapping epitopes that preferentially drive binding to tumor cells and a low-affinity anti-CD47 arm to enable avidity-induced blocking of proximal CD47 receptors. We previously reported the pharmacology of ISB 1442, designed to reestablish synthetic immunity in CD38+ hematological malignancies.

View Article and Find Full Text PDF

Structure and self-association of Arrestin-1.

J Struct Biol

January 2025

Gavin Herbert Eye Institute - Center for Translational Vision Research, Department of Ophthalmology, University of California, Irvine, CA 92697, USA; Department of Chemistry, University of California, Irvine, CA 92697, USA; Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA. Electronic address:

Arrestins halt cell signaling by binding to phosphorylated activated G protein-coupled receptors. Arrestin-1 binds to rhodopsin, arrestin-4 binds to cone opsins, and arrestins-2,3 bind to the rest of GPCRs. In addition, it has been reported that arrestin-1 is functionally expressed in mouse cone photoreceptors.

View Article and Find Full Text PDF

A conserved chaperone protein is required for the formation of a non-canonical type VI secretion system spike tip complex.

J Biol Chem

January 2025

Department of Biochemistry and Biomedical Sciences, McMaster University, 1280 Main Street West, Hamilton, Ontario, Canada L8S 4K1; Michael DeGroote Institute for Infectious Disease Research, McMaster University, Hamilton, Ontario, Canada L8S 4K1. Electronic address:

Type VI secretion systems (T6SS) are dynamic protein nanomachines found in Gram-negative bacteria that deliver toxic effector proteins into target cells in a contact-dependent manner. Prior to secretion, many T6SS effector proteins require chaperones and/or accessory proteins for proper loading onto the structural components of the T6SS apparatus. However, despite their established importance, the precise molecular function of several T6SS accessory protein families remains unclear.

View Article and Find Full Text PDF

Characterization and formation of the biomineral aragonite structures of the Noah's Ark shell ( L.,1758) were studied from structural, morphogenetic, and biochemical points of view. Structural and morphological features were examined using X-ray diffraction, field-emission scanning electron microscopy, and atomic force microscopy, while thermal properties were determined by thermogravimetric and differential thermal analyses.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!