Sequence and initial characterization of the U L 10 (glycoprotein M) and U L 11 homologous genes of serotype 1 Marek’s Disease Virus

Sequence and initial characterization of the U L 10 (glycoprotein M) and U L 11 homologous genes... The nucleotide sequence of the U L 10 (glycoprotein M) and the U L 11 homologs of Marek’s Disease Virus 1 strain GA was determined. The U L 10 open reading frame encodes a type III membrane protein of 424 amino acids that contains eight hydrophobic domains and two consensus N-linked glycosylation sites. The U L 11 homologous gene encodes an 84 amino acid polypeptide, and contains a highly conserved myristylation site at its aminoterminus. By analysis of infected-cell RNA with strand-specific RNA probes, transcription of both U L 10 and U L 11 in infected cells was demonstrated. Coupled in vitro transcription-translation confirmed that the U L 10 product is a 47 kD N-glycosylated viral protein that aggregated upon boiling, whereas the U L 11 protein exhibited a size of 12 kD after in vitro translation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Sequence and initial characterization of the U L 10 (glycoprotein M) and U L 11 homologous genes of serotype 1 Marek’s Disease Virus

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Publisher
Springer Journals
Copyright
Copyright © Wien by 1999 Springer-Verlag/
Subject
Legacy
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s007050050710
Publisher site
See Article on Publisher Site

Abstract

The nucleotide sequence of the U L 10 (glycoprotein M) and the U L 11 homologs of Marek’s Disease Virus 1 strain GA was determined. The U L 10 open reading frame encodes a type III membrane protein of 424 amino acids that contains eight hydrophobic domains and two consensus N-linked glycosylation sites. The U L 11 homologous gene encodes an 84 amino acid polypeptide, and contains a highly conserved myristylation site at its aminoterminus. By analysis of infected-cell RNA with strand-specific RNA probes, transcription of both U L 10 and U L 11 in infected cells was demonstrated. Coupled in vitro transcription-translation confirmed that the U L 10 product is a 47 kD N-glycosylated viral protein that aggregated upon boiling, whereas the U L 11 protein exhibited a size of 12 kD after in vitro translation.

Journal

Archives of VirologySpringer Journals

Published: Sep 1, 1999

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