Insect Plasma Proteins

Wyatt, G.R.; Pan, M. L.

doi:10.1146/annurev.bi.47.070178.004023

Cited by 287 publications

(68 citation statements)

References 103 publications

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“…Haemolymph lipoproteins have been identified in several insect species, in particular silkmoths, locusts, and cockroaches (cf. Wyatt and Pan, 1978). In Lepidoptera, two major DG-transporting lipoproteins were identified in Hyalophora cecropia and H. gloveri Gilbert, 1968, 1969), and in Philosamia cynthia (Chino et al, 1969).…”

Section: Lipid Transportmentioning

confidence: 99%

Insect flight muscle metabolism

Beenakkers

Horst

Marrewijk

1984

Insect Biochemistry

225

130

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Section: Lipid Transportmentioning

confidence: 99%

Insect flight muscle metabolism

Beenakkers

Horst

Marrewijk

1984

Insect Biochemistry

225

130

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“…Arylphorin is a high M r (approx. 450K) hexameric plasma protein of lepidopteran insects which has a high content of aromatic amino acids (Wyatt & Pan, 1978;Kanost et al, 1990). This protein accumulates to high concentrations in the haemolymph of larvae, and may constitute 70 to 80 % of the total plasma protein in the penultimate larval instar (LeClerc & Miller, 1990).…”

Section: Introductionmentioning

confidence: 99%

Polydnavirus infection inhibits synthesis of an insect plasma protein, arylphorin

Shelby

Webb

1994

Journal of General Virology

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The wasp Campoletis sonorensis injects a segmented, double-stranded DNA polydnavirus (CsPDV) along with its egg during parasitization of Heliothis virescens larvae. After parasitization, CsPDV protects the wasp egg and larva by selectively disabling the host's cellular immune response. Other host physiological systems including growth and development are affected to the apparent benefit of the parasite. To begin the characterization of the biochemical effects and mode of action of CsPDV on host growth, the titre of a developmentally regulated insect storage protein, arylphorin, was studied. Parasitized or virus-infected insects had substantially less circulating arylphorin than control insects. Fat bodies from parasitized larvae also synthesized less arylphorin in vitro. However, Northern blots of total RNA from parasitized and non-parasitized, control insects showed that the arylphorin transcript level was unaffected by parasitization suggesting a biochemical block at the translational level. In vitro translation followed by immunoprecipitation ofarylphorin indicated that the mRNA was present and translatable at equal levels in both parasitized and control insects. Injection of purified virus elicited the response observed in naturally parasitized larvae, demonstrating that the effect on arylphorin synthesis is mediated, either directly or indirectly, by polydnavirus gene product(s).

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“…Work in a number of systems has shown that the vitellogenins are synthesized in the liver of vertebrates (1,2) and in the fat body of insects (3). After secretion, the vitellogenins are transported to the ovary via the blood and converted into the yolk proteins by the oocyte.…”

mentioning

confidence: 99%

Two processing steps in maturation of vitellogenin polypeptides in Drosophila melanogaster.

Warren¹,

Brennan²,

Mahowald³

1979

Proc. Natl. Acad. Sci. U.S.A.

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Synthesis of the three vitellogenin polypeptides (molecular weights of 44,000,45,000, and 46,000) of Drosophila melanogaster has been analyzed in vivo and in a cell-free system. After labeling periods in vivo, the three vitellogenin polypeptides were made as the principal synthetic products of the female fat body. During a short (0.5 min) labeling period, they were identified as discrete species on two-dimensional gels. Two of the polypeptides have molecular weights of 45,000 and a third has a molecular weight of 44,000. After longer labeling periods (5-45 min) the three mature vitellogenins appeared. Both immunoprecipitation and peptide mapping confirmed that the species labeled at 0.5 min are immature forms of the vitellogenin polypeptides. In vitro translation of poly(A)RNA from female fat body indicated another processing step in vitellogenin synthesis. Three polypeptides were obtained that were identified as precursors of the vitellogenins on the basis of immunoprecipitation and peptide mapping. Two of the translation products have a molecular weight of 46,000 and the third has a molecular weight of 45,000. Because the vitellogenins are secreted proteins, we interpret the higher molecular weight of the in vitro translation products as being due to signal peptides.

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Insect Plasma Proteins

Cited by 287 publications

References 103 publications

Insect flight muscle metabolism

Insect flight muscle metabolism

Polydnavirus infection inhibits synthesis of an insect plasma protein, arylphorin

Two processing steps in maturation of vitellogenin polypeptides in Drosophila melanogaster.

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