Gossypol is a constituent of the lysigenous foliar glands of cotton plants and is also found in glands in cottonseed. Gossypol exists as enantiomers because of restricted rotation around the binaphthyl bond. The biological activities of the enantiomers differ. For example, (+)-gossypol can be fed safely to nonruminants such as chickens, but (-)-gossypol cannot. Most commercial cottonseed contain a (+)- to (-)-gossypol ratio of approximately 3:2. Conventional breeding techniques can be used to develop cottonseed that contains >95% (+)-gossypol. Notably, gossypol protects the plant from insect herbivores. Herein, we report the effect of various forms of gossypol on Heliothis virescens (Fabricius) larvae. Three levels (0.16, 0.24, and 0.32%) of racemic, (+)-, and (-)-gossypol were added to artificial rearing diets and were fed to H. virescens larvae. All 0.24 and 0.32% gossypol diets significantly lengthened days-to-pupation and decreased pupal weight compared with the control. Percent survival was significantly less for larvae reared on diets containing 0.24% of all three forms of gossypol as compared with the control diet. (+)-Gossypol was superior or equivalent to racemic gossypol as measured by the three parameters studied. Higher concentrations of all gossypol forms were required to reduce survival and pupal weights and increase days-to-pupation for larvae of H. virescens larvae compared with the concentration needed to affect larvae of Helicoverpa zea (Boddie), which was studied previously. These results indicate that current efforts to breed cotton lines containing mostly (+)-gossypol in seed should not significantly impair the plant's natural defenses against insects.
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http://dx.doi.org/10.1603/0046-225X(2008)37[1081:EORAGO]2.0.CO;2 | DOI Listing |
Pestic Biochem Physiol
September 2024
Hunan Provincial Key Laboratory for Biology and Control of Plant Diseases and Insect Pests, Hunan Agricultural University, Changsha, Hunan 410128, PR China; College of Plant Protection, Hunan Agricultural University, Changsha, Hunan 410128, PR China. Electronic address:
Sci Rep
November 2023
Institute for Biodiversity and Ecosystem Dynamics, University of Amsterdam, Amsterdam, The Netherlands.
Sexual signals often function in species recognition and may also guide mate choice within a species. In noctuid moths, both males and females may exercise mate choice. Females of the tobacco budworm Chloridea virescens prefer to mate with larger males, but the signal(s) underlying female choice remain unknown.
View Article and Find Full Text PDFMicrobiol Spectr
December 2023
Hunan Provincial Key Laboratory for Biology and Control of Plant Diseases and Insect Pests, College of Plant Protection, Hunan Agricultural University, Changsha, Hunan, China.
Different pathogenic processes of a virus in different hosts are related to the host individual differences, which makes the virus undergoes different survival pressures. Here, we found that the virions of an insect virus, Heliothis virescens ascovirus 3h (HvAV-3h), had different protein composition when they were purified from different host larval species. These "adaptive changes" of the virions were analyzed in detail in this study, which mainly included the differences of the protein composition of virions and the differences in affinity between virions and different host proteins.
View Article and Find Full Text PDFBiomolecules
October 2023
Department of Sciences, University of Basilicata, Via dell'Ateneo Lucano 10, 85100 Potenza, Italy.
Arch Insect Biochem Physiol
October 2023
UMR 152 Pharma-Dev, Faculté des Sciences Pharmaceutiques, Institut de Recherche et Développement, Université Toulouse 3, Toulouse, France.
Heliothis virescens larval chymotrypsin (GenBank accession number AF43709) was cloned, sequenced and its three dimensional (3D) conformation modeled. The enzyme's transcript was first detected 6 days after larval emergence and the transcript level was shown to fall between larval ecdysis periods. Comparisons between the activities of larval gut chymotrypsin and trypsin shows that chymotrypsin activity is only 16% of the total trypsin activity and the pH optimum of the larval chymotrypsin is between pH 9-10, however the enzyme also exhibited a broad activity between pH 4-6.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!