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PubMed1977

Membrane fractions from the outer layers of spores of Bacillus thuringiensis with toxicity to lepidopterous larvae.

Two membrane fractions, F1 and F2, have been purified from the outer layers of spores of Bacillus thuringiensis. Both fractions contain 6-7% cysteine and appear to be similar in composition. Amino acids account for about 75% of the dry weight, carbohydrate for about 2% and lipids for about 25%. The fractions are both toxic to Pieris brassicae and the toxicity is inactivated by antiserum to the toxic crystal of Bacillus thuringiensis. The fractions can be distinguished by examination under the electron microscope; both fractions show similar hexagonal patterns but with different spacings. The same fractions from an acrystaliferous mutant (cr) were prepared. These were identical in density and in appearance under the electron microscope; the amino acid analysis of fraction F2 from both strains was identical. However, the spores and fractions F1 and F2 from this strain lacked toxicity. Fraction F2 from the cr strain was used to prepare antiserum specific to fraction F2. Using this anti-serum and anticrystal serum, crystal and F2 antigens were shown to appear simultaneously in sporulating cultures. Crystal and F2 antigens appeared some time before the maximum rate of uptake of [35s]cysteine. It is concluded that fraction F2 is derived from the exosporium and that fraction F1 probably originates from the spore coat. The exosporium in Bacillus thuringiensis appears to be synthesised during stages II and III of sporulation although uptake of [35S]cysteine occurs much later.

Amino Acids↗
PubMed1979

Lepidopterism.

Explore the source record for details and available documents.

Animals↗
PubMed2026

Venomous Lepidoptera: defensive toxin systems, venom composition, and clinical significance.

Venomous Lepidoptera constitute an underrecognized yet medically significant group of toxin-producing arthropods that employ contact-mediated defensive envenomation through specialized integumentary structures such as setae, spines, and scoli. Unlike actively stinging arthropods, these insects deliver venom passively upon contact, eliciting a diverse spectrum of clinical manifestations collectively termed lepidopterism. Clinical outcomes range from localized pain and dermatitis to severe systemic effects, including hemorrhagic syndromes, complement activation, and chronic inflammatory disorders. Recent advances in proteomic and transcriptomic technologies have transformed our understanding of lepidopteran venoms, revealing unexpectedly complex toxin repertoires comprising serine proteases, phospholipases, pore-forming proteins, disulfide-rich peptides, neuroactive RF-amide peptides, and immune-modulating components. These findings have provided new insights into the molecular basis of toxicity, host-pathogen interactions, and the evolutionary diversification of venom systems within Lepidoptera. This review synthesizes current knowledge on the morphology of venom-delivery structures, venom composition, mechanisms of action, and associated clinical manifestations, while highlighting medically important taxa, particularly species of the genus Lonomia. The successful development of antivenom against Lonomia envenomation underscores the translational relevance of lepidopteran toxin research and its potential for therapeutic innovation. By integrating molecular, clinical, and evolutionary perspectives, this review repositions venomous Lepidoptera as a legitimate and important component of arthropod toxinology. Furthermore, it identifies critical methodological limitations and key knowledge gaps, providing a framework for future investigations aimed at advancing our understanding of toxin biology, immunopathology, and the development of novel biomedical applications.

Animals↗
PubMed1975

An insect toxin from spores of Bacillus thuringiensis and Bacillus cereus.

Spores of Bacillus thuringiensis contain a toxin active against lepidopterous larvae. This toxin can be solubilized by extraction with reagents which dissolve the protein crystal of B thuringiensis. It is inactivated by crystal-specific antiserum. Spores of Bacillus cereus contain a similar toxin although the specific activity is much lower than the spores of B. thuringiensis. The B. cereus toxin contains a single major polypeptidecomponent. Toxic activity can be solubliized from spores of both species by incubation with gut juices from Pieris brassicae.

Amino Acids↗
PubMed1978

An insect cell line persistently infected with a baculovirus-like particle.

A persistent infection by a baculovirus-like particle was found in the established lepidopteran (Heliothis zea) cell line, IMC-HZ-1. The virus caused CPE in less than 1% of the IMC-HZ-1 cells, as measured by phase-contrast and electron microscopy. Transmission tests showed that four lepidopteran cell lines were susceptible to the persistent virus (designated as IMC-HZ-I-NOV). In inoculated TN-368 cell cultures, 90--100% infection was achieved. The ultrastructure and development of IMC-HZ-I-NOV in cell cultures were similar to known baculoviruses, and it is probable that this persistent virus is a member of the family Baculoviridae. Two lepidopterous species (Estigmene acrea and H. zea) inoculated with IMC-HZ-1-NOV by intrahemocoelic injection and/or per os feeding of larvae were not susceptible.

Cell Line↗
PubMed1975

Skin-piercing blood-sucking moths I: ecological and ethological studies on Calpe eustrigata (Lepid., noctuidae).

The Noctuid Calpe [Calyptral] eustrigata Hmps. was reported as a skin-piercing blood-sucking moth for the first time in Malaya (Bänziger, 1968) and is so far the only lepidopteran proved to suck blood by means of a piercing act. A few field observations and the description of the piercing behaviour of caged moths were given. Apart from a taxonomic study of the genus Calpe (Berio, 1956), a single record (Büttiker, 1969) and some notes on the moth's proboscis and possible evolutionary pathway (Bänziger, 1970, 1971, 1972) to our knowledge no other data have been published on the moth after its description as a new species (Hampson, 1926). The life cycle is completely unknown. From the scanty museum specimens available, it appears that the species inhabits South and Southeast Asia. A closely related, though less rare species, the fruit-piercing C. thalictri Bkh., has been used for a detailed study of the piercing mechanism likely to be adopted by Calpe (Bänziger, 1970); the feeding turned out to be as unusual as the feeding habits. Little or nothing is known about other Calpe species. C. eustrigata is not the only adult lepidopterous parasite of mammals. Lachryphagous ("eye-frequenting") moths feed as "marginal" parasites upon eye-secretions of ungulates, elephants and occasionally man (Shannon, 1928; Reid, 1954; Büttiker, 1964, 1967; Bänziger, 1966). Arcyophora species and the eulachryphagous Noctuid Lobocraspis graseifusa Hmps. which apparently feeds exclusively upon eye discharges, are suspected as vectors of eye diseases (Guilbride et al., 1959, Büttiker, 1964; Bänziger, 1972). While no lachryphagous moth is able to suck blood by a piercing act, there are a number of facultative lachryphagous moths which lick up the blood freely present at wounds, or that excreted anally by mosquitoes (Bänziger, 1969, 1972). Because of the scientific interest in C. eustrigata, research has been carried out to investigate different biological aspects of the species in Malaysia, Thailand. Laos and Indonesia (May 1971-May 1973). The first account presented here will be continued with a paper (in prep.) on the piercing mechanism and soon, it is hoped, with more information on the physiology, life cycle and medical importance of the moth.

Adaptation, Biological↗
PubMed1977

Some experimental observations on the cryptonephric malpighian tubules.

Imago of Tenebrio, Dermestes (Coleoptera) and Lepidopterous caterpillars Pieris and Galleria were observed for the general physiology of the cryptonephric Malpighian tubules. Injection of dyes were made. The dyes were taken only by the free portion of the Malpighian tubules. Reassociated Malpighian tubules do not take dyes from the haemoly mph. They are secretory, but not excretory. The perinephric membrane in the Lepidoptera is impermeable to the dyes.

Animals↗