Toxicity and Binding Studies of Bacillus thuringiensis Cry1Ac, Cry1F, Cry1C, and Cry2A Proteins in the Soybean Pests Anticarsia gemmatalis and Chrysodeixis (Pseudoplusia) includens.

(velvetbean caterpillar) and (soybean looper, formerly named ) are two important defoliating insects of soybeans. Both lepidopteran pests are controlled mainly with synthetic insecticides. Alternative control strategies, such as biopesticides based on the (Bt) toxins or transgenic plants expressing Bt toxins, can be used and are increasingly being adopted.

Insecticidal Toxin Complexes from Photorhabdus luminescens.

Various bacterial toxins have potent insecticidal activity. Recently, the Toxin complexes (Tc's) of Photorhabdus and Xenorhabdus species have become an increased focus of current research. These large tripartite toxins with molecular masses >1.

Field-Evolved Mode 1 Resistance of the Fall Armyworm to Transgenic Cry1Fa-Expressing Corn Associated with Reduced Cry1Fa Toxin Binding and Midgut Alkaline Phosphatase Expression.

Insecticidal protein genes from the bacterium Bacillus thuringiensis (Bt) are expressed by transgenic Bt crops (Bt crops) for effective and environmentally safe pest control. The development of resistance to these insecticidal proteins is considered the most serious threat to the sustainability of Bt crops. Resistance in fall armyworm (Spodoptera frugiperda) populations from Puerto Rico to transgenic corn producing the Cry1Fa insecticidal protein resulted, for the first time in the United States, in practical resistance, and Bt corn was withdrawn from the local market.

Insecticidal activity of Bacillus thuringiensis Cry1Bh1 against Ostrinia nubilalis (Hubner) (Lepidoptera: Crambidae) and other lepidopteran pests.

Bacillus thuringiensis is an important source of insect resistance traits in commercial crops. In an effort to prolong B. thuringiensis trait durability, insect resistance management programs often include combinations of insecticidal proteins that are not cross resistant or have demonstrable differences in their site of action as a means to mitigate the development of resistant insect populations.

Insecticidal toxin complex proteins from Xenorhabdus nematophilus: structure and pore formation.

Toxin complexes from Xenorhabdus and Photorhabdus spp. bacteria represent novel insecticidal proteins. We purified a native toxin complex (toxin complex 1) from Xenorhabdus nematophilus.

Targeting of the actin cytoskeleton by insecticidal toxins from Photorhabdus luminescens.

Photorhabdus luminescens produces several types of protein toxins, which are essential for participation in a trilateral symbiosis with nematodes and insects. The nematodes, carrying the bacteria, invade insect larvae and release the bacteria, which kill the insects with their toxins. Recently, the molecular mechanisms of the toxin complexes PTC3 and PTC5 have been elucidated.

Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering.

The bacterium Photorhabdus luminescens is mutualistically associated with entomopathogenetic nematodes. These nematodes invade insect larvae and release the bacteria from their intestine, which kills the insects through the action of toxin complexes. We elucidated the mode of action of two of these insecticidal toxins from P.

Ronald Estabrook's early guidance of a postdoctoral fellow concerning the intricacies of steroid metabolism by cytochromes P450.

Ronald Estabrook made his initial impact studying cytochrome P450 by demonstrating the oxidative metabolism function of this unique class of enzymes, which had an unusual spectral peak at 450 nm when reduced and in the presence of carbon monoxide. Utilizing a photochemical action spectrum, he demonstrated that a cytochrome P450 was responsible for steroid 21 hydroxylation catalyzed by microsomes prepared from adrenal cortex tissue. As a young postdoctoral student, I was given the unique opportunity to learn from a true pioneer in this field.

Laboratory performance and pharmacokinetics of the benzoylphenylurea noviflumuron in eastern subterranean termites (Isoptera: Rhinotermitidae).

A benzoylphenylurea insect growth regulator with the common name noviflumuron was evaluated for use as a baiting toxicant against the eastern subterranean termite, Reticulitermes flavipes (Kollar). Noviflumuron demonstrated significantly greater potency and faster speed of action compared with the commercial standard hexaflumuron. In addition, noviflumuron was not a feeding deterrent on filter paper at concentrations of up to 10,000 ppm.