Bruce Christian Black

Commercialization of Baculoviral Insecticides

The commercialization of baculoviruses has had a long and checkered history. Early insect virologists were quick to see the potential of these highly infectious and selective pathogens. This, in addition to the safety of these agents, proved irresistibly attractive for the development of these viruses as insecticides. During the 1970s, the first baculoviral product was introduced into the commercial arena, Elcar [Helicoverpa zea nuclear polyhedrosis virus (NPV)]. This product was accompanied by three noncommercial preparations produced by the US Forestry Service, namely Gypcheck (Lymantria dispar NPV), TM BioControl-1 (Orgyia pseudotsuga NPV), and Neocheck-S (Neodiprion sertifer NPV). During these early days, products suffered from a variety of problems, including variable potency, high production costs, poor formulation, and generally inferior field performance when compared to chemical alternatives. Eventually, production of these viral insecticides ceased with the exception of Gypcheck.

Linkage of pyrethroid insecticide resistance to a sodium channel locus in the tobacco budworm

Pyrethroids, with their lack of persistence and low mammalian toxicity, have been important insecticides since the early 1970s. However, heavy use has selected for resistance to pyrethroids in populations of many insects, in particular the tobacco budworm Heliothis virescens, a major cotton pest in the Americas. Several studies have identified the voltage-gated sodium channel as the principal target of pyrethroid action, and the sodium channel has been implicated in pyrethroid resistance in Musca domestica and Drosophila melanogaster. We present molecular genetic evidence that pyrethroid resistance is linked to a sodium channel locus in a strain of H. virescens. This is the first such evidence for any major agricultural pest, and is an important step towards understanding the molecular basis of resistance. This in turn will facilitate assessment, modeling, and control of resistance in pest populations, and increase our understanding of sodium channel function.

The genetics of dopa decarboxylase in Drosophila melanogaster. IV. The genetics and cytology of the 37B10-37D1 region.

Of 204 mutations located in the 8-12 band Df(2L)130 region, 37B9-C1,2;37D1-2, 199 have been assigned to twelve lethal genes and one visible gene (hook). The 13 genes are not evenly distributed. Twelve, (possibly all thirteen) are in the seven band region 37B10-C4 giving a gene-to-band ratio of almost two. Only one gene, 1(2)37Cf, may be in the four band region 37C5-7, and none are localized in band 37D1. In situ hybridization places the dopa decarboxylase structural gene, Ddc, in or very close to band 37C1,2 (Hirsh and Davidson, 1981). The chi methyl dopa hypersensitive gene, 1(2) and, is 0.002 map units distal to Ddc. Df(2L)VA17, 37C1,2; 37F5-38A1 may actually break in the 37C1,2 singlet. It places six genes, hook, 1(2) and, and four lethal genes, in a maximum of five bands, 37B10, 11, 12, 13 and perhaps part of the 37C1,2 singlet and localizes six genes, Ddc plus five lethal genes, in a maximum of three bands; probably part of the 37C1,2 singlet plus bands, C3, and C4. Wild type activity of five of twelve lethal genes is necessary for female fertility. --Band 37C5 puffs at the time of pupariation; Puff Stages 8-10. Twelve of eighteen alleles of 1(2)37Cf have been examined as heterozygotes over CyO and none affect the appearance of a homozygous 37C5 puff. --Of the 204 mutations considered here only one Ddcpl, affects the function of more than one gene. It eliminates Ddc+ and 1(2)37Ca+ function and at 30 degrees C reduces 1(2)37Ce+ function. It is not a deficiency but could be a polar mutant.

Mutations affecting phenol oxidase activity inDrosophila: quicksilver andtyrosinase-1

The complex enzyme phenol oxidase plays a major role in sclerotization and melanization of cuticle in insects. Production of active enzyme from the inactive proenzyme involves at least six protein components inDrosophila. We examine here the biochemical phenotype of two loci that affect phenol oxidase activity—quicksilver (qs; 1–39.5) andtyrosinase-1 (tyr-1; 2–54.5). Three mutations isolated by different procedures in three different laboratories are alleles at thequicksilver locus. The effects of these mutations have been monitored by means of enzyme assaysin vitro and in polyacrylamide gels and by measurement of catecholamine pool sizes. The activity of all three active enzyme components (A1, A2, and A3) is reduced inqs mutants. The activated enzyme of oneqs allele is thermolabile, while its activator is normal. Deletion and genetic mapping placetyr-1 nearpurple (pr; 2–54.5). Enzyme activity is reduced to 10% of normal but is not thermolabile and the activator is normal. The activity of all three A components is reduced. The diphenol oxidase activity in double mutant combinations shows that these mutations andDox-A2 (Pentzet al., 1986) affect this enzyme in different ways.