Expression of neuroparsin cDNA in insect cells using baculovirus vectors.

Arch Insect Biochem Physiol

Laboratoire de Neuroendocrinologie, URA CNRS 1138, Université Bordeaux I, Talence, France.

Published: September 1997

AI Article Synopsis

  • The study inserted the cDNA for neuroparsin A, a neurohormone from locusts, into a virus genome to produce this protein in infected cells.
  • The resulting polypeptide matched the authentic neuroparsin in charge and molecular weight and was recognized by antibodies specific to neuroparsin.
  • Additionally, the expressed polypeptide improved fluid reabsorption in lab experiments, confirming its functional similarity to natural neuroparsin.

Article Abstract

The cDNA encoding neuroparsin A, a polytropic neurohormone of the locust, Locusta migratoria, was inserted into the genome of Autographa californica nuclear polyhedrosis virus such that transcription was under control of the p10 promoter. A polypeptide having the same charge and the same apparent molecular weight as the authentic neuroparsin A and that was reactive against neuroparsin immune serum was produced in recombinant virus-infected lepidopteran cell lines but not in control virus-infected cells. The baculovirus-expressed polypeptide was purified by two steps of liquid chromatography (anion exchange and reversed phase) which were previously used to purify the natural neuroparsin. The purified baculovirus-expressed polypeptide enhanced fluid reabsorption of everted rectum preparations, as did the natural neuroparsin. Thus, this gene expression system produced a polypeptide identical to authentic neuroparsin.

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http://dx.doi.org/10.1002/(SICI)1520-6327(1997)36:1<11::AID-ARCH2>3.0.CO;2-ZDOI Listing

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Expression of neuroparsin cDNA in insect cells using baculovirus vectors.

Arch Insect Biochem Physiol

September 1997

Laboratoire de Neuroendocrinologie, URA CNRS 1138, Université Bordeaux I, Talence, France.

Article Synopsis
  • The study inserted the cDNA for neuroparsin A, a neurohormone from locusts, into a virus genome to produce this protein in infected cells.
  • The resulting polypeptide matched the authentic neuroparsin in charge and molecular weight and was recognized by antibodies specific to neuroparsin.
  • Additionally, the expressed polypeptide improved fluid reabsorption in lab experiments, confirming its functional similarity to natural neuroparsin.
View Article and Find Full Text PDF

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