GP96 Interacts with HHV-6 during Viral Entry and Directs It for Cellular Degradation

Here, we used a proteomics approach to identify other host cell proteins necessary for HHV-6 binding and entry. ABLASHI, S.Z. 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. Human herpesvirus 6B (HHV-6B) is a betaherpesvirus. Infectivity assay results of Vero cells illustrated that the drug-induced disruption of lipid rafts significantly suppressed IBV infection. Human herpesvirus 6B (HHV-6B) is a betaherpesvirus. Infectivity assay results of Vero cells illustrated that the drug-induced disruption of lipid rafts significantly suppressed IBV infection.

Yamanishi, J. In the nearly 30 years since their discovery, we have only begun to unlock the molecular strategies these highly evolved pathogens employ to establish and maintain chronic infections in humans. Accepted receptor criteria are met through the use of function-blocking integrin Abs, β1 integrin knockout mouse fibroblasts, and glycoprotein B disintegrin-like peptides, all of which support a critical role for α2β1, α6β1, and αVβ3 integrins as HCMV entry receptors and signaling mediators acting during the penetration stage of the entry pathway. As early as 5 min p.i., KSHV infection induced the recruitment of activated c-Cbl and myosin IIA to the bleb regions [29]. Cells expressing individual CMV glycoproteins did not form multinucleated syncytia. Furthermore, we demonstrated a close association of incoming HCMV capsids with MTs by IFA and ultrastructural analyses. 1) HSPG, a widely expressed and evolutionary conserved cell surface receptor, is suggested as the initial attachment receptor for HPVs and is frequently found in the ECM and on the surface of most cells.

1b,c). For this reason, the study of sugar chains should be promoted to control infectious diseases. Lack of ATP1A1 did not affect virus binding to host cells but resulted in inhibited entry of MHV and VSV. With the exception of EBV [3] which uses the cellular receptor CD21 (or CR2) for attachment [4], all oncogenic viruses initially attach to their target cells via ubiquitously expressed cell membrane heparan sulfate proteoglycans (HSPG), also termed the “universal receptor”, which contain charged carbohydrate moieties that can interact with several viral surface glycoproteins or protein ligands expressed in the envelope and/or the capsid, respectively. ..Our findings suggest that mature HHV-6 virions are released together with internal vesicles through MVBs by the cellular exosomal pathway. Addition of gp120 caused polarized cocapping of both molecules with subsequent pseudopod formation, while CytoD pretreatment blocked these membrane changes completely. Here, I review our current knowledge regarding herpesvirus entry into host cells and virus assembly…

The 20 FH SCR domains are illustrated in the context of their binding specificities for N. 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. Importantly, these early studies demonstrated that even infants with subclinical or silent infections could develop neurological sequelae (Stagno et al., 1982, 1983; Williamson et al., 1992). However, details of the interaction between the HHV-6B gH/gL/gQ1/gQ2 complex and CD134 were unknown. In addition, the ganglioside GM1, which is known to partition preferentially into lipid rafts, was detected in purified virions, along with viral envelope glycoproteins, gH, gL, gB, gQ1, gQ2 and gO indicating that at least one raft component was included in the viral particle during the assembly process. Often, the role of the cellular environment that is critical for the complex process of virus uptake has taken a back stage. But many cell types interfere with viral infection through rapid degradation of viral DNA.

We observed that virus spread in fibroblast cultures was predominantly supernatant-driven, whereas spread in endothelial cell (EC) cultures was predominantly focal. The olfactory bulb/tract samples from 20 subjects with an unspecified encephalopathy determined by pathomorphological examination of the brain autopsy, 17 healthy age-matched and 16 younger controls were used. We have identified a viral glycoprotein, UL148, that influences the cell tropism of HCMV virions by regulating the relative amounts of these two gH/gL complexes. Here, we used a proteomics approach to identify other host cell proteins necessary for HHV-6 binding and entry. In general, enveloped viruses are highly dependent on their lipid envelope for entry into host cells. Here we show that Ebola virus-like particles (EBOV-VLPs) composed of the glycoprotein GP1,2 and the matrix protein VP40 use macropinocytosis and clathrin-mediated endocytosis to enter cells. It has been difficult to study infection of these cell types because HCMV laboratory strains (e.g., AD169 and Towne) have lost their ability to infect cultured epithelial and endothelial cells during extensive propagation in fibroblasts.

Previous studies suggest roles for clathrin- or caveolae-mediated endocytosis in EBOV entry; however, ebolavirus virions are long, filamentous particles that are larger than the plasma membrane invaginations that characterize clathrin- or caveolae-mediated endocytosis. House Oversight Committee Chairman Rep. Articles in JID include research results from microbiology, immunology, epidemiology, and related disciplines. of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo 060, Japan.

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