The characterization and purification of DNA binding proteins present within herpes simplex virus infected cells using monoclonal antibodies

The characterization and purification of DNA binding proteins present within herpes simplex virus infected cells using monoclonal antibodies

The organization of encapsidated herpes simplex viral DNA in situ was examined by use of the osmium-amine stain specific for DNA. Comparison of different HSV VP16 sequences reveals a conserved core region that is sufficient for VP16-induced complex formation. Herpes simplex virus (HSV), varicella-zoster virus (VZV), and pseudorabies virus (PRV) all utilize a complex of two glycoproteins, gE and gI, to move from cell to cell. The “moving wall” represents the time period between the last issue available in JSTOR and the most recently published issue of a journal. VII. Cell Biol.72, 194–208 (1977). These results indicate that disulfide cross-links are normally present in extracellular virions but not in intracellular capsids.

Thus, HSV-1 VP22 is a significant neurovirulence factor in vivo. Challberg, J. Nature New Biol.231, 139–142 (1971). Like other alphaherpesviruses, HSV-1 has the ability to establish lifelong infections or latency in neurons within the peripheral nervous system of its human host. T., Ponce de Leon, M., Pereira, L., Long, D., Cohen, G. H.: Purification of gylcoprotein gD of herpes simplex virus types 1 and 2 by use of monoclonal antibody. Consistent with its location in the tegument, it has been shown that VP16 is required for proper viral assembly and egress (Mossman et al., 2000).

The characterization and purification of DNA binding proteins present within herpes simplex virus infected cells using monoclonal antibodies
Virol.41, 1099–1104 (1982). la Thangue, N. The structure and assembly of the VP16-induced complex has been studied extensively. Granzow, R. D.: Monoclonal antibodies to herpes simplex type 1 glycoproteins show that epitope location influences virus neutralization. J. Med.

During the next round of infection, capsids are released into the cytoplasm, traffic to the nucleus, and dock at a nuclear pore, at which point they undergo a disassembly process resulting in the release of viral DNA into the nucleus (58, 71). Leiden, J. M., Buttyman, R., Spear, P.: Herpes simplex virus gene expression in transformed cells: regulation of the thymidine kinase gene in transformed L cells by products of superinfecting virus. J. During entry of PrV, the inner tegument proteins VP1/2 (pUL36) and pUL37 have been shown to remain associated with the incoming capsids, while outer tegument proteins, such as VP13/14 (pUL47), VP16 (pUL48), and VP22 (pUL49), dissociate during PrV entry into nonneuronal cells (18) and chick sensory neurons (38). Wilcox, K. W., Kohn, A., Sklyanskay, E., Roizman, B.: Herpes simplex virus phosphoproteins.

Similarly, deletion of gD, gE, and gI in HSV-1 has recently been shown to cause a major defect in assembly, resulting in accumulation of unenveloped capsids in the cytoplasm that are embedded in tegument-like material. Phosphate cycles on and off some viral polypeptides and can alter their affinity for DNA. J. VP16 is a modular protein of 490 amino acids. E-mail: johnsoda{at}ohsu.edu. J., Rabin, H., Hopkins, R. F., Neubauer, R.

H., Hampar, B.: Production of monoclonal antibodies against nucleocapsid proteins of herpes simplex virus types 1 and 2. A polyclonal antibody (ID1) against UL25 raised against a glutathione S-transferase-UL25 fusion protein was provided by Nels Pederson (East Carolina University School of Medicine). Virol.32, 676–678 (1979).

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