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We found host cell chaperone protein GP96 to interact with HHV-6A and HHV-6B and to interfere with virus propagation within the host cell. SALAHUDDIN, A. In human peripheral blood mononuclear cells (PBMCs), GP96 is transported to the cell surface upon infection with HHV-6 and interacts with HHV-6A and -6B through its C-terminal end. Initially, HHV-6B and HHV-6A were classified as two variants of HHV-6; however, they are now classified as two virus species due to their different bio-characteristics (1,–5). Further studies revealed that lipid rafts were not required for IBV genome replication or virion release at later stages. Initially, HHV-6B and HHV-6A were classified as two variants of HHV-6; however, they are now classified as two virus species due to their different bio-characteristics (1,–5). Further studies revealed that lipid rafts were not required for IBV genome replication or virion release at later stages.

Virol. The aims of this review are to provide an overview of roseolovirus molecular biology and highlight recent advances in our understanding of the molecular basis of the virus lifecycle, which in turn inform our understanding of pathogenesis, and illuminate paths to diagnosis, treatment, and prevention. Strikingly, the glycoprotein B disintegrin-like domain is conserved in many human and animal herpesviruses, suggesting that integrins may support entry across this medically important virus family. c-Cbl-myosin IIA interaction and c-Cbl mediated myosin IIA ubiquitination is essential for bleb mediated macropinocytosis of KSHV in HMVEC-d cells as knockdown of c-Cbl results in the inhibition of virus entry by macropinocytosis [29].Soon after KSHV binding to the HS and integrins, infection induced PI3-K activates c-Cbl, which in turn mediates differential ubiquitination of viral entry receptor to regulate the virus entry pathways and their fate [30]. Conversely, cells expressing gH/gL showed pronounced syncytium formation, although expression of gH or gL alone had no effect. In the absence of the MT network, the capsids which had entered the cytoplasm did not move to close proximity of the nucleus. HPV capsids have also been shown to bind to ECM-resident laminin-5 although this interaction seems to be of lesser importance for a productive infection.

In cell–cell fusion assays with epithelial cells, intact E1D1 showed a significant inhibition at the lowest concentrations tested, while the E1D1 Fab showed a dose-dependent inhibition (Fig. This paper describes the importance of viral glycobiology and states the necessity to develop and foster a new research field, “glycovirology”, incorporating recent studies by the author’s research group and others. Consistently, nanomolar concentrations of the cardiotonic steroids ouabain and bufalin, which are known not to affect the transport function of Na+,K+-ATPase, inhibited infection of cells with MHV, FIPV, Middle East respiratory syndrome (MERS)-CoV, and VSV, but not IAV, when the compounds were present during virus inoculation. This leads to accumulation of the viral particle at the cell surface and is generally followed by conformational changes ultimately facilitating viral uptake by secondary cell type- and/or virus-specific receptors. This scenario has significant implications for understanding HHV-6’s maturation pathway… Elucidation of the mechanism of virus selection of, and entry into, suitable host cells is a key to understanding human immunodeficiency virus (HIV) transmission and pathogenesis. ..These data suggest that gamma-PGA-NPs may have potential for clinical applications as a mucosal adjuvant…

… In human peripheral blood mononuclear cells (PBMCs), GP96 is transported to the cell surface upon infection with HHV-6 and interacts with HHV-6A and -6B through its C-terminal end. In the late 1960s, HCMV was recognized as a significant cause of disease in allograft recipients and in the case of hematopoietic allograft recipients, HCMV infection became recognized as one of the most frequent causes of death in the post-transplant period (Rifkind, 1965; Myers et al., 1975; Ho, 1977; Rubin et al., 1979; Winston et al., 1979; Rubin et al., 1981; Rubin and Colvin, 1986; Rubin, 1990). In this study, we identified a cysteine-rich domain (CRD), CDR2, of CD134 that is critical for binding to the HHV-6B glycoprotein complex and HHV-6B infection. Interestingly, most of the viruses associated with AIDS cause tumors. Hence, not all cells expressing these receptors are permissive to HHV-6 DNA replication and production of infective virions suggesting the involvement of additional factors that influence HHV-6 propagation. This was due to properties of virus released from fibroblasts and EC.

HHV-6 DNA was detected in 60, 29, and 19% of cases in these groups, respectively. Our findings have implications for understanding how herpesviruses navigate through host tissues. We found host cell chaperone protein GP96 to interact with HHV-6A and HHV-6B and to interfere with virus propagation within the host cell. Here, we demonstrated that during the course of virus maturation, a significant proportion of human herpesvirus 6 (HHV-6) envelope proteins were selectively concentrated in the detergent-resistant glycosphingolipid- and cholesterol-rich membranes (rafts) in HHV-6-infected cells. EBOV-VLPs applied to host cells induced actin-driven ruffling and enhanced FITC-dextran uptake, which indicated macropinocytosis as the main entry mechanism.