Human Herpesvirus 6 immediate-early 1 protein is a sumoylated nuclear phosphoprotein colocalizing with promyelocytic leukemia protein-associated nuclear bodies.

The Journal of Biological Chemistry
Annie GravelLouis Flamand

Abstract

Immediate-early (IE) proteins are the first proteins expressed following viral entry and play a crucial role in the initiation of infection. We report the cloning and characterization of a full-length IE1 transcript and protein (IE1B) from human herpesvirus 6 (HHV-6) variant B. The IE1B transcript consists of five exons (3720 nucleotides), three of which are coding for the IE1 protein. The 1078-amino acid-long IE1B protein is 62% identical and 75% similar to the 941-amino acid IE1 from HHV-6 variant A. IE1B protein can be detected at 4 h post-infection (P.I.), and it is distributed as small intranuclear structures. The maximal number of IE1 bodies ( approximately 10-12/nucleus) is detected at 12 h P.I. after which the IE1 bodies condense into 1-3 larger entities by 24-48 h P.I. During infection the IE1B protein is phosphorylated on serine and threonine residues. IE1B undergoes further post-translational modification with its conjugation to the small ubiquitin-like modifier (SUMO-1) peptide. IE1B colocalizes with SUMO-1 and promyelocytic leukemia nuclear bodies during infection as well as in transfection experiments. Finally, IE1 from variant B is a weaker transactivator than IE1 from variant A, when assayed using heterologous p...Continue Reading

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Citations

Oct 3, 2003·Journal of Clinical Virology : the Official Publication of the Pan American Society for Clinical Virology·Suzie ArsenaultLouis Flamand
Apr 21, 2010·Proceedings of the National Academy of Sciences of the United States of America·Joanna JaworskaLouis Flamand
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