11/21/2023 0 Comments Dot blot apparatur![]() Weed DJ, Dollery SJ, Komala Sari T, Nicola AV (2018) Acidic pH mediates changes in antigenic and oligomeric conformation of herpes simplex virus gB and is a determinant of cell-specific entry. Virol J 7:352ĭollery SJ, Wright CC, Johnson DC, Nicola AV (2011) Low-pH-dependent changes in the conformation and oligomeric state of the prefusion form of herpes simplex virus glycoprotein B are separable from fusion activity. Siekavizza-Robles CR, Dollery SJ, Nicola AV (2010) Reversible conformational change in herpes simplex virus glycoprotein B with fusion-from-without activity is triggered by mildly acidic pH. Nicola AV (2016) Herpesvirus entry into host cells mediated by endosomal low pH. Weed DJ, Pritchard SM, Gonzalez F, Aguilar HC, Nicola AV (2017) Mildly acidic pH triggers an irreversible conformational change in the fusion domain of herpes simplex virus 1 glycoprotein B and inactivation of viral entry. Roller DG, Dollery SJ, Doyle JL, Nicola AV (2008) Structure-function analysis of herpes simplex virus glycoprotein B with fusion-from-without activity. Adv Anat Embryol Cell Biol 223:29–47ĭollery SJ, Delboy MG, Nicola AV (2010) Low pH-induced conformational change in herpes simplex virus glycoprotein B. Weed DJ, Nicola AV (2017) Herpes simplex virus membrane fusion. Nicola AV, Straus SE (2004) Cellular and viral requirements for rapid endocytic entry of herpes simplex virus. Johnson DC, Ligas MW (1988) Herpes simplex viruses lacking glycoprotein D are unable to inhibit virus penetration: quantitative evidence for virus-specific cell surface receptors. J Virol 62(8):2596–2604įorrester A et al (1992) Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted. J Clin Pharmacol 47(12):1570–1579Ĭai WH, Gu B, Person S (1988) Role of glycoprotein B of herpes simplex virus type 1 in viral entry and cell fusion. Warnke D, Barreto J, Temesgen Z (2007) Antiretroviral drugs. White JM, Whittaker GR (2016) Fusion of enveloped viruses in endosomes. Nicola AV, Aguilar HC, Mercer J, Ryckman B, Wiethoff CM (2013) Virus entry by endocytosis. This method can be adapted to document changes in viral proteins that are not fusion proteins, including those induced by alternate triggers such as receptor-binding or protease cleavage. Many of the identified changes are at least partially reversible. This corresponds broadly to host cell endosomal pH. At pH of <6.2 there are specific changes in herpes simplex virus 1 gB domains I and V. This dot blot technique has been utilized to define low pH-triggered changes in the prefusion form of the herpesviral fusogen gB. Here we describe a simple and rapid virus blotting immunoassay to define conformational changes with a panel of monoclonal antibodies to distinct sites across a viral glycoprotein. ![]() Conformational changes in viral membrane proteins drive membrane fusion, a critical step in virus entry and infection.
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