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Forest Sciences

University of Nebraska - Lincoln

1994

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Full-Text Articles in Life Sciences

Identification And Characterization Of The Ecdysteroid Udpglucosyltransferase Gene Of The Lymantria Dispar Multinucleocapsid Nuclear Polyhedrosis Virus, Christopher I. Riegel, Carita Lanner-Herrera, James M. Slavicek Jan 1994

Identification And Characterization Of The Ecdysteroid Udpglucosyltransferase Gene Of The Lymantria Dispar Multinucleocapsid Nuclear Polyhedrosis Virus, Christopher I. Riegel, Carita Lanner-Herrera, James M. Slavicek

United States Department of Agriculture, Forest Service / University of Nebraska-Lincoln: Faculty Publications

We have located, cloned, sequenced and characterized the ecdysteroid UDP-glucosyltransferase gene (egt) gene from the baculovirus Lymantria dispar multinucleocapsid nuclear polyhedrosis virus,(LdMNPV), which is specific for the gypsy moth (L. dispar). The egt gene from the related baculovirus Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV) disrupts the hormonal balance of the host larva by galactosylating ecdysone, which prevents moulting. The location of the LdMNPV egt gene, determined by hybridization analysis using a cloned coding segment of the AcMNPV egt gene, was mapped to between 79.1 and 80.2 map units on the viral genome. This region contains an open …


Identification And Characterization Of A Protein Kinase Gene In The Lymantria Dispar Multinucleocapsid Nuclear Polyhedrosis Virus, David S. Bischoff, James M. Slavicek Jan 1994

Identification And Characterization Of A Protein Kinase Gene In The Lymantria Dispar Multinucleocapsid Nuclear Polyhedrosis Virus, David S. Bischoff, James M. Slavicek

United States Department of Agriculture, Forest Service / University of Nebraska-Lincoln: Faculty Publications

The Lymantria dispar multinucleocapsid nuclear polyhedrosis virus (LdMNPV) gene encoding vPK has been cloned and sequenced. LdMNPV vPK shows a 24% amino acid identity to the catalytic domains of the eucaryotic protein kinases nPKC from rabbits, HSPKCE from humans, APLPKCB from Aplysia californica, and dPKC98F from Drosophila melanogaster, and homology to several other protein kinases from yeasts, mice, and bovines. The homology suggests that vPK is a serine/threonine protein kinase as defined by Hanks et al. (S. K. Hanks, A. M. Quinn, and T. Hunter, Science 241:42-52, 1988). Temporal expression studies indicate that vPK is expressed throughout the …