Seroreactivity to Kaposi's sarcoma-associated herpesvirus (human herpesvirus 8) latent nuclear antigen in AIDS-associated Kaposi's sarcoma patients depends on CD4+ T-cell count

2007 ◽  
Vol 79 (10) ◽  
pp. 1562-1568 ◽  
Author(s):  
Vanda Akico Ueda Fick de Souza ◽  
Ligia Camera Pierrotti ◽  
Laura Masami Sumita ◽  
Wilton Santos Freire ◽  
Aluisio Augusto Cotrim Segurado ◽  
...  
Keyword(s):  
T Cell ◽  
Kaposi's Sarcoma ◽  
Human Herpesvirus ◽  
Kaposi’S Sarcoma ◽  
Cd4 T Cell ◽  
Human Herpesvirus 8 ◽  
Nuclear Antigen ◽  
Herpesvirus 8 ◽  
Latent Nuclear Antigen ◽  
Cd4 T Cell Count

scholarly journals Characterization of Monoclonal Antibodies Raised against the Latent Nuclear Antigen of Human Herpesvirus 8

1999 ◽  
Vol 73 (6) ◽  
pp. 5149-5155 ◽  
Author(s):  
Paul Kellam ◽  
Dimitra Bourboulia ◽  
Nicolas Dupin ◽  
Chris Shotton ◽  
Cyril Fisher ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Kaposi's Sarcoma ◽  
Human Herpesvirus ◽  
Kaposi’S Sarcoma ◽  
Human Herpesvirus 8 ◽  
Nuclear Antigen ◽  
Viral Gene ◽  
Herpesvirus 8 ◽  
Latent Nuclear Antigen

ABSTRACT Human herpesvirus 8 (HHV-8; also designated Kaposi’s sarcoma-associated herpesvirus) is the likely etiological agent of Kaposi’s sarcoma (KS). HHV-8 encodes a latent nuclear antigen (LNA) which is the product of the viral gene orf 73. LNA is recognized by most infected patient sera and is the basis of current immunofluorescence assays used in epidemiological studies of HHV-8 infection. Here we describe the characterization of four monoclonal antibodies raised to the C-terminal third of LNA–glutathioneS-transferase fusion proteins. These monoclonal antibodies recognized discrete linear epitopes within the C terminus and repetitive region of LNA, detected antigen in primary effusion lymphoma (PEL) cells, and precipitated a 220- to 230-kDa protein doublet corresponding to LNA from HHV-8-infected PEL cell lines. In situ immunocytochemistry of KS lesions with these antibodies show that LNA is extensively expressed in KS spindle cells.

scholarly journals Regulatory T Cell Effect on CD8+T Cell Responses to Human Herpesvirus 8 Infection and Development of Kaposi's Sarcoma

2017 ◽  
Vol 33 (7) ◽  
pp. 668-674 ◽  
Author(s):  
Lauren M. Lepone ◽  
Giovanna Rappocciolo ◽  
Paolo A. Piazza ◽  
Diana M. Campbell ◽  
Frank J. Jenkins ◽  
...  
Keyword(s):  
T Cell ◽  
Regulatory T Cell ◽  
Kaposi's Sarcoma ◽  
Human Herpesvirus ◽  
T Cell Responses ◽  
Kaposi’S Sarcoma ◽  
Cd8 T Cell ◽  
Human Herpesvirus 8 ◽  
Herpesvirus 8 ◽  
Cell Responses

scholarly journals Carboxy Terminus of Human Herpesvirus 8 Latency-Associated Nuclear Antigen Mediates Dimerization, Transcriptional Repression, and Targeting to Nuclear Bodies

2000 ◽  
Vol 74 (18) ◽  
pp. 8532-8540 ◽  
Author(s):  
David R. Schwam ◽  
Randy L. Luciano ◽  
Shahana S. Mahajan ◽  
LaiYee Wong ◽  
Angus C. Wilson
Keyword(s):  
Kaposi's Sarcoma ◽  
Human Herpesvirus ◽  
Kaposi’S Sarcoma ◽  
Nuclear Bodies ◽  
Human Herpesvirus 8 ◽  
Nuclear Antigen ◽  
Intact Protein ◽  
Viral Gene ◽  
Herpesvirus 8 ◽  
C Terminus

ABSTRACT Human herpesvirus 8 (HHV-8; also known as Kaposi's sarcoma-associated herpesvirus) is the causative agent of Kaposi's sarcoma and certain B-cell lymphomas. In most infected cells, HHV-8 establishes a latent infection characterized by the expression of latency-associated nuclear antigen (LANA) encoded by open reading frame 73. Although unrelated by sequence, there are functional similarities between LANA and the EBNA-1 protein of Epstein-Barr virus. Both accumulate as subnuclear speckles and are required for maintenance of the viral episome. EBNA-1 also regulates viral gene expression and is required for cell immortalization, suggesting that LANA performs similar functions in the context of HHV-8 infection. Here we show that LANA forms stable dimers, or possibly higher-order multimers, and that this is mediated by a conserved region in the C terminus. By expressing a series of truncations, we show that both the N- and C-terminal regions localize to the nucleus, although only the C terminus accumulates as nuclear speckles characteristic of the intact protein. Lastly, we show that LANA can function as a potent transcriptional repressor when tethered to constitutively active promoters via a heterologous DNA-binding domain. Domains in both the N and C termini mediate repression. This suggests that one function of LANA is to suppress the expression of the viral lytic genes or cellular genes involved in the antiviral response.

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