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001 ocn773727090;

003 OCoLC;

005 20141212075947.0;

006 m d ;

007 cr bn|||||||||;

008 120124s2011 ncua ob 000 0 eng d;

035 a| (Sirsi) o773727090;

035 a| (OCoLC)773727090;

040 a| EREc| EREd| EREd| UtOrBLW;

049 a| EREE;

090 a| QP552.G59;

100 1 a| Walker, Lia R.?| UNAUTHORIZED;

245 10 a| Disintegrin-like domain in KSHV encoded gB is a necessity to promote virus latency /c| by Lia R. Walker.;

260 a| [Greenville, N.C.] :b| East Carolina University,c| 2011.;

300 a| 80 pages :b| illustrations (some color), digital, PDF file;

336 a| text2| rdacontent;

337 a| computer2| rdamedia;

338 a| online resource2| rdacarrier;

538 a| System requirements: Adobe Reader.;

538 a| Mode of access: World Wide Web.;

502 b| M.S.c| East Carolina Universityd| 2011.;

500 a| Presented to the faculty of the Department of Biology.;

500 a| Advisor: Shaw Akula.;

500 a| Title from PDF t.p. (viewed Mar. 8, 2012).;

520 3 a| KSHV glycoprotein B (gB) is a lytic structural protein expressed on the envelope of mature virions and on the membrane of cells supporting lytic infection. Previous studies have identified that in addition to the role of envelope-associated gB in virus binding, entry, and egress, cell membrane-bound gB has a role in promoting cellular attachment and virus latency, suggesting its involvement in KSHV pathogenesis. In addition to the more common integrin recognition motif, RGD (Arg-Gly-Asp), KSHV gB uniquely possesses a disintegrin-like domain (DLD). DLD is known to exert anti-integrin effects. In order to understand the role of DLD in gB, we generated recombinant gB lacking a functional DLD and tested it in biochemical and functional assays. Here we provide evidence demonstrating the role of DLD in regulating the function of gB-induced signaling critical to suppressing virus reactivation. Through screening phage display peptide library, [alpha]9[beta]1, a non-RGD binding integrin, was identified as a potential receptor for the DLD in KSHV gB. However, gB with an intact DLD can still exert its inhibitory effects on virus reactivation in 293 cells that do not express [alpha]9 integrins; possibly via other [beta]1 integrins. Such findings are an asset to further understand the biology of gB--especially in terms of appreciating roles of different domains within the same protein critical for its net function in the virulence.;

504 a| Includes bibliographical references.;

650 0 a| Glycoproteins.=| ^A8952;

650 0 a| Kaposi's sarcoma.=| ^A708280;

650 0 a| Herpesvirus diseases.=| ^A126582;

653 a| Biology;

700 1 a| Akula, Shaw M.=| ^A1406820;

710 2 a| East Carolina University.b| Department of Biology.=| ^A637467;

856 40 z| Access via ScholarShipu| http://hdl.handle.net/10342/3714;

949 o| jgml;

994 a| C0b| ERE;

596 a| 1 4;

998 a| 2677551;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2677551-1001l| JNETm| JOYNERr| Ys| Yt| JNE3ETDu| 1/24/2012x| ETDz| JERESOURCE;

999 a| CLICK ON WEB ADDRESSw| ASISc| 1i| 2677551-2001l| HSLELECm| HSLr| Ys| Yt| HEETDu| 1/24/2012x| ETDz| HERESOURCE;

Disintegrin-like domain in KSHV encoded gB is a necessity to promote virus latency / by Lia R. Walker.

Author/creator	Walker, Lia R.
Other author	Akula, Shaw M.
Other author	East Carolina University. Department of Biology.
Format	Theses and dissertations
Publication Info	[Greenville, N.C.] : East Carolina University, 2011.
Description	80 pages : illustrations (some color), digital, PDF file
Supplemental Content	Access via ScholarShip
Subjects	Glycoproteins. Kaposi's sarcoma. Herpesvirus diseases.

Summary	KSHV glycoprotein B (gB) is a lytic structural protein expressed on the envelope of mature virions and on the membrane of cells supporting lytic infection. Previous studies have identified that in addition to the role of envelope-associated gB in virus binding, entry, and egress, cell membrane-bound gB has a role in promoting cellular attachment and virus latency, suggesting its involvement in KSHV pathogenesis. In addition to the more common integrin recognition motif, RGD (Arg-Gly-Asp), KSHV gB uniquely possesses a disintegrin-like domain (DLD). DLD is known to exert anti-integrin effects. In order to understand the role of DLD in gB, we generated recombinant gB lacking a functional DLD and tested it in biochemical and functional assays. Here we provide evidence demonstrating the role of DLD in regulating the function of gB-induced signaling critical to suppressing virus reactivation. Through screening phage display peptide library, [alpha]9[beta]1, a non-RGD binding integrin, was identified as a potential receptor for the DLD in KSHV gB. However, gB with an intact DLD can still exert its inhibitory effects on virus reactivation in 293 cells that do not express [alpha]9 integrins; possibly via other [beta]1 integrins. Such findings are an asset to further understand the biology of gB--especially in terms of appreciating roles of different domains within the same protein critical for its net function in the virulence.
General note	Presented to the faculty of the Department of Biology.
General note	Advisor: Shaw Akula.
General note	Title from PDF t.p. (viewed Mar. 8, 2012).
Dissertation note	M.S. East Carolina University 2011.
Bibliography note	Includes bibliographical references.
Technical details	System requirements: Adobe Reader.
Technical details	Mode of access: World Wide Web.

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Disintegrin-like domain in KSHV encoded gB is a necessity to promote virus latency / by Lia R. Walker.

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