scholarly journals Synergy between Kaposi's sarcoma-associated herpesvirus (KSHV) vIL-6 and HIV-1 Nef protein in promotion of angiogenesis and oncogenesis: role of the AKT signaling pathway

Oncogene ◽  
2013 ◽  
Vol 33 (15) ◽  
pp. 1986-1996 ◽  
Author(s):  
X Zhu ◽  
Y Guo ◽  
S Yao ◽  
Q Yan ◽  
M Xue ◽  
...  
Keyword(s):  
Signaling Pathway ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Akt Signaling ◽  
Akt Signaling Pathway ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Hiv 1

scholarly journals Role of Kaposi's Sarcoma-Associated Herpesvirus C-Terminal LANA Chromosome Binding in Episome Persistence

2009 ◽  
Vol 83 (9) ◽  
pp. 4326-4337 ◽  
Author(s):  
Brenna Kelley-Clarke ◽  
Erika De Leon-Vazquez ◽  
Katherine Slain ◽  
Andrew J. Barbera ◽  
Kenneth M. Kaye
Keyword(s):  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Chromosome Association ◽  
Mitotic Chromosomes ◽  
Dividing Cells ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Self Association ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Chromosome Binding

ABSTRACT Kaposi's sarcoma-associated herpesvirus (KSHV) LANA is an 1,162-amino-acid protein that tethers terminal repeat (TR) DNA to mitotic chromosomes to mediate episome persistence in dividing cells. C-terminal LANA self-associates to bind TR DNA. LANA contains independent N- and C-terminal chromosome binding regions. N-terminal LANA binds histones H2A/H2B to attach to chromosomes, and this binding is essential for episome persistence. We now investigate the role of C-terminal chromosome binding in LANA function. Alanine substitutions for LANA residues 1068LKK1070 and 1125SHP1127 severely impaired chromosome binding but did not reduce the other C-terminal LANA functions of self-association or DNA binding. The 1068LKK1070 and 1125SHP1127 substitutions did not reduce LANA's inhibition of RB1-induced growth arrest, transactivation of the CDK2 promoter, or C-terminal LANA's inhibition of p53 activation of the BAX promoter. When N-terminal LANA was wild type, the 1068LKK1070 and 1125SHP1127 substitutions also did not reduce LANA chromosome association or episome persistence. However, when N-terminal LANA binding to chromosomes was modestly diminished, the substitutions in 1068LKK1070 and 1125SHP1127 dramatically reduced both LANA chromosome association and episome persistence. These data suggest a model in which N- and C-terminal LANA cooperatively associates with chromosomes to mediate full-length LANA chromosome binding and viral persistence.

scholarly journals Role of Host MicroRNAs in Kaposi’s Sarcoma-Associated Herpesvirus Pathogenesis

Viruses ◽  
2014 ◽  
Vol 6 (11) ◽  
pp. 4571-4580 ◽  
Author(s):  
Zhiqiang Qin ◽  
Francesca Peruzzi ◽  
Krzysztof Reiss ◽  
Lu Dai
Keyword(s):  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus

scholarly journals Molecular Mechanism of BST2/Tetherin Downregulation by K5/MIR2 of Kaposi's Sarcoma-Associated Herpesvirus

2009 ◽  
Vol 83 (19) ◽  
pp. 9672-9681 ◽  
Author(s):  
Mandana Mansouri ◽  
Kasinath Viswanathan ◽  
Janet L. Douglas ◽  
Jennie Hines ◽  
Jean Gustin ◽  
...  
Keyword(s):  
Kaposi's Sarcoma ◽  
Defense Mechanism ◽  
Transmembrane Protein ◽  
Kaposi’S Sarcoma ◽  
Dependent Manner ◽  
Type Ii ◽  
Amino Terminal ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Hiv 1

ABSTRACT K3/MIR1 and K5/MIR2 of Kaposi's sarcoma-associated herpesvirus (KSHV) are viral members of the membrane-associated RING-CH (MARCH) ubiquitin ligase family and contribute to viral immune evasion by directing the conjugation of ubiquitin to immunostimulatory transmembrane proteins. In a quantitative proteomic screen for novel host cell proteins downregulated by viral immunomodulators, we previously observed that K5, as well as the human immunodeficiency virus type 1 (HIV-1) immunomodulator VPU, reduced steady-state levels of bone marrow stromal cell antigen 2 (BST2; also called CD317 or tetherin), suggesting that BST2 might be a novel substrate of K5 and VPU. Recent work revealed that in the absence of VPU, HIV-1 virions are tethered to the plasma membrane in BST2-expressing HeLa cells. By targeting BST2, K5 might thus similarly overcome an innate antiviral host defense mechanism. Here we establish that despite its type II transmembrane topology and carboxy-terminal glycosylphosphatidylinositol (GPI) anchor, BST2 represents a bona fide target of K5 that is downregulated during primary infection by and reactivation of KSHV. Upon exit of the protein from the endoplasmic reticulum, lysines in the short amino-terminal domain of BST2 are ubiquitinated by K5, resulting in rapid degradation of BST2. Ubiquitination of BST2 is required for degradation, since BST2 lacking cytosolic lysines was K5 resistant and ubiquitin depletion by proteasome inhibitors restored BST2 surface expression. Thus, BST2 represents the first type II transmembrane protein targeted by K5 and the first example of a protein that is both ubiquitinated and GPI linked. We further demonstrate that KSHV release is decreased in the absence of K5 in a BST2-dependent manner, suggesting that K5 contributes to the evasion of intracellular antiviral defense programs.

Risk factors for Kaposi's sarcoma-associated herpesvirus infection among HIV-1-infected pregnant women in the USA

AIDS ◽  
2003 ◽  
Vol 17 (3) ◽  
pp. 425-433 ◽  
Author(s):  
James J Goedert ◽  
Manhattan Charurat ◽  
William A Blattner ◽  
Ronald C Hershow ◽  
Jane Pitt ◽  
...  
Keyword(s):  
Risk Factors ◽  
Pregnant Women ◽  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Herpesvirus Infection ◽  
The Usa ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Hiv 1

scholarly journals Assembly of infectious Kaposi’s sarcoma-associated herpesvirus progeny requires formation of a pORF19 pentamer

PLoS Biology ◽  
2021 ◽  
Vol 19 (11) ◽  
pp. e3001423
Author(s):  
Peter Naniima ◽  
Eleonora Naimo ◽  
Sandra Koch ◽  
Ute Curth ◽  
Khaled R. Alkharsah ◽  
...  
Keyword(s):  
Kaposi's Sarcoma ◽  
Kaposi’S Sarcoma ◽  
Structural Similarity ◽  
Capsid Assembly ◽  
Genome Packaging ◽  
Infected Cells ◽  
Kaposi's Sarcoma Associated Herpesvirus ◽  
Kaposi’S Sarcoma Associated Herpesvirus ◽  
Novel Drug

Herpesviruses cause severe diseases particularly in immunocompromised patients. Both genome packaging and release from the capsid require a unique portal channel occupying one of the 12 capsid vertices. Here, we report the 2.6 Å crystal structure of the pentameric pORF19 of the γ-herpesvirus Kaposi’s sarcoma-associated herpesvirus (KSHV) resembling the portal cap that seals this portal channel. We also present the structure of its β-herpesviral ortholog, revealing a striking structural similarity to its α- and γ-herpesviral counterparts despite apparent differences in capsid association. We demonstrate pORF19 pentamer formation in solution and provide insights into how pentamerization is triggered in infected cells. Mutagenesis in its lateral interfaces blocked pORF19 pentamerization and severely affected KSHV capsid assembly and production of infectious progeny. Our results pave the way to better understand the role of pORF19 in capsid assembly and identify a potential novel drug target for the treatment of herpesvirus-induced diseases.

Sign in / Sign up

Export Citation Format

Share Document