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Functional properties of Epstein-Bar...

Lynch, David T.

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Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2).

Record Type:	Electronic resources : Monograph/item
Title/Author:	Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2)./
Author:	Lynch, David T.
Description:	152 p.
Notes:	Source: Dissertation Abstracts International, Volume: 63-05, Section: B, page: 2212.
Contained By:	Dissertation Abstracts International63-05B.
Subject:	Biology, Molecular. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3054304
ISBN:	0493695877

Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2).
Lynch, David T.

Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2). - 152 p.

Source: Dissertation Abstracts International, Volume: 63-05, Section: B, page: 2212.

Thesis (Ph.D.)--University of Pittsburgh, 2002.

Epstein Barr virus (EBV) is a lymphotropic human herpesvirus which is the causative agent of infectious mononucleosis (IM) and is associated with several human malignancies. Messenger RNA from the Latent Membrane Protein two (LMP2) gene of EBV is the only mRNA consistently detected in latently infected B cells from healthy carriers.

ISBN: 0493695877Subjects--Topical Terms:

1017719
Biology, Molecular.

Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2).
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100 1 $a Lynch, David T. $3 1900081
245 1 0 $a Functional properties of Epstein-Barr virus (EBV) latent membrane protein 2 (LMP2).
300 $a 152 p.
500 $a Source: Dissertation Abstracts International, Volume: 63-05, Section: B, page: 2212.
500 $a Adviser: David T. Rowe.
502 $a Thesis (Ph.D.)--University of Pittsburgh, 2002.
520 $a Epstein Barr virus (EBV) is a lymphotropic human herpesvirus which is the causative agent of infectious mononucleosis (IM) and is associated with several human malignancies. Messenger RNA from the Latent Membrane Protein two (LMP2) gene of EBV is the only mRNA consistently detected in latently infected B cells from healthy carriers.
520 $a The LMP2 gene of Epstein-Barr virus encodes two protein isoforms of 497aa (LMP2A) and 378aa (LMP2B) which are distinguished by an additional 119aa N-terminal signaling domain encoded by the first exon of LMP2A.
520 $a In these studies, we evaluated the effects of serine phosphorylation on protein-protein interactions <italic>in vitro</italic>, using GST fusions of the LMP2A cytoplasmic domain containing S15 and S102 point mutants. Our results demonstrate that point mutants converting S102 to aspartic acid (D) greatly affect the LMP2A-exon1 affinities for MAPK and ubiquitin ligases and highlight the importance of this site as a potential regulator of LMP2A function <italic> in vivo</italic>.
520 $a The focus of LMP2 research to date has been on the biochemical properties of the LMP2A cytoplasmic domain. A plasma membrane orientation for LMP2 have been widely assumed. However, there has been no in depth analysis of protein localization or the functional significance of the conserved 12 transmembrane structure shared by both LMP2 isoforms. These studies have been difficult because of the hydrophobic nature of the proteins and the lack of effective immunological reagents to detect the proteins in biochemical assays. Using fluorescent and epitope-tagged LMP2, we demonstrate that the proteins localize to perinuclear regions of transient expressing cells. We have mapped the subcellular localization of LMP2 by respect of immunofluorescence using markers specific for cellular membrane compartments. Recombinant LMP2 exhibits a high level of association with the trans-Golgi marker γ-adaptin. No colocalization was observed between LMP2 and B cell surface markers. LMP2A and LMP2B were found to colocalize in EBV(+) and EBV(−) LCLs. Fluorescence microscopy of C-terminally truncated LMP2A mutants reveal that the perinuclear localization observed with full length proteins is likely conferred by sequences or structural elements in the last six transmembrane segments. Furthermore, truncated LMP2A proteins specifically co localize with full length LMP2B protein when transiently co-expressed. (Abstract shortened by UMI.)
590 $a School code: 0178.
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Microbiology. $3 1017734
690 $a 0307
690 $a 0410
710 2 0 $a University of Pittsburgh. $3 958527
773 0 $t Dissertation Abstracts International $g 63-05B.
790 1 0 $a Rowe, David T., $e advisor
790 $a 0178
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3054304