Insecticidal Activity of Chitinases from HB310 and Its Relationship with the Toxin Complex.

HB310 secreted the insecticidal protein toxin complex (Tc). The and chitinase genes are located on the gene cluster encoding Tc toxins. To clarify the insecticidal activity of chitinases and their relationship with Tc toxins, the insecticidal activity of the chitinases was assessed on .

Functional characterization of a novel, highly expressed ion-driven sugar antiporter in the thoracic muscles of Helicoverpa armigera.

Sugar transporters (STs), which mainly mediate cellular sugar exchanges, play critical physiological roles in living organisms, and they may be responsible for sugar exchanges among various insect tissues. However, the molecular and physiological functions of insect STs are largely unknown. Here, 16 STs of Helicoverpa armigera were identified.

Expression and characterization of two chitinases with synergistic effect and antifungal activity from Xenorhabdus nematophila.

Xenorhabdus nematophila HB310 secreted the insecticidal protein toxin complex. Two chitinase genes, chi60 and chi70, were found in X. nematophila toxin complex locus.

Characteristics and Function of the Chitin Binding Protein from .

Background: Genome sequence analysis (GenBank access No.: FN667742.1) shows that ATCC19061 contains one gene (Xn-cbp) encoding chitin binding protein (Xn-CBP).

PirAB protein from Xenorhabdus nematophila HB310 exhibits a binary toxin with insecticidal activity and cytotoxicity in Galleria mellonella.

PirAB (Photorhabdus insect-related proteins, PirAB) toxin was initially found in the Photorhabdus luminescens TT01 strain and has been shown to be a binary toxin with high insecticidal activity. Based on GenBank data, this gene was also found in the Xenorhabdus nematophila genome sequence. The predicted amino acid sequence of pirA and pirB in the genome of X.

Aminopeptidase N5 (APN5) as a Putative Functional Receptor of Cry1Ac Toxin in the Larvae of Athetis lepigone.

Athetis lepigone was a new lepidopteran pest and caused severe damage to maize crops in China. We have detected that Cry1Ac protoxin and toxin were highly active against the larvae of A. lepigone.

Detection of minimum activity fragment of a novel Cry7Ab3 protein specific to Henosepilachna vigintioctomaculata (Coleopteran: Coccinellidae).

Bacillus thuringiensis Cry7Ab3 toxin has insecticidal activity against larvae of Henosepilachna vigintioctomaculata. Cry7Ab3 toxin is solubilized under alkaline condition and activated by proteases within the larval gut. In order to assess the functions of the N- and C-terminal regions, several N- and C-terminal truncated forms of Cry7Ab3 were constructed.

Identification of Henosepilachna vigintioctomaculata (Coleoptera: Coccinellidae) midgut putative receptor for Bacillus thuringiensis insecticidal Cry7Ab3 toxin.

Bt WZ-9 strain, containing a single Cry7Ab3 toxin, had effective insecticidal activity against larvae of Henosepilachna vigintioctomaculata. By incubation with larvae midgut homogenate and trypsin in vitro, 130 kDa Cry7Ab3 protoxin was degraded into the ∼75 kDa proteinase-resistant fragments. In vivo analysis, 130 kDa Cry7Ab3 protoxin was also processed into ∼75 kDa fragment.

[Purification and characterization of the haemocoel insecticide Tp40 from Xenorhabdus nematophila].

Objective: Xenorhabdus nematophila is an insect pathogen bacterium symbiotically associated with entomopathogenic nematode. The bacteria produce a number of toxins to overcome immune response of insect hosts and kill their hosts. We purified a novel haemocoel insecticidal protein from X.