Anti-KSHV ORF26 Monoclonal antibody

The association between Human Herpes Virus-8 (HHV-8), also called Kaposi's sarcoma associated herpesvirus (KSHV), and the pathogenesis of multiple myeloma remains controversial. Many past studies conducting on different populations have come to contradicting conclusions. In this study, we attempted to investigate the presence of HHV-8 in Jordanian multiple myeloma patients. We carried out nucleic acid amplification reactions targeting specific viral DNA sequences on 35 fresh bone marrow aspirate samples from 17 patients with multiple myeloma, 9 patients with various hematological malignancies and 9 normal subjects. HHV-8 specific sequences were detected in 7 out of 17 multiple myeloma patients (41%) using primers specific for the open reading frame region 26 (ORF26). All patients with other hematological malignancies as well as the normal subjects did not harbour the virus. These findings support the previous reports of frequent detection of HHV-8 in bone marrow of multiple myeloma patients. (C) 2010 Elsevier Ltd. All rights reserved.

Herpesvirus virions are highly organized structures built through specific protein-protein interactions. Thus, revelation of the protein interactions among virion proteins will shed light on the processes and the mechanisms of virion formation. Recently, we identified 24 virion proteins of Kaposi's sarcoma-associated herpesvirus (KSHV), using a proteomic approach (F. X. Zhu et al., J. Virol. 79:800-811, 2005). In the current study, a comprehensive analysis of protein-protein interaction between KSHV virion proteins was carried out using yeast two-hybrid (Y2H) and coimmunoprecipitation (co-IP) approaches. Every pairwise combination between KSHV tegument and capsid proteins, between tegument and envelope proteins, and among tegument proteins was tested for possible binary interaction. Thirty-seven protein-protein interactions were identified by both Y2H and co-IP analyses. The results revealed interactions between tegument and capsid proteins such as that of open reading frame 64 (ORF64) with ORF25 (major capsid protein [MCPI), ORF62 (triplex-1 [TRI-1]), and ORF26 (TRI-2). Many interactions were detected among the tegument proteins. ORF64 was found to interact with several tegument proteins including ORF11, ORF21, ORF33, ORF45, ORF63, ORF75, and ORF64 itself, suggesting that ORF64 may serve as a hub protein and play a role in recruiting tegument proteins during tegumentation and virion assembly. Our investigation also revealed redundant interactions between tegument proteins and envelope glycoproteins. These interactions are believed to contribute to final envelopment in virion assembly. Overall, this study allows us to establish a virion-wide protein interaction map, which provides insight into the architecture of the KSHV virion and sets up a foundation for exploring the functions of these proteins in viral particle assembly.