Studies on the in vitro uncoating of poliovirus II. Characteristics of the membrane-modified particle
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Cited by (99)
Enterovirus entry and uncoating
2023, Molecular Medical Microbiology, Third EditionEnteroviruses: The role of receptors in viral pathogenesis
2022, Advances in Virus ResearchCitation Excerpt :Although the precise role of the pocket factor is enterovirus uncoating remained unclear, more recent structural studies suggest that it plays an active role in structural rearrangements of the capsid that occur near sites of receptor binding on the canyon (Lee et al., 2016). The process of uncoating triggers conformational changes in VP1 leading to the externalization of its N-terminus (Fricks and Hogle, 1990) as well as the release of VP4 from the capsid altogether (Crowell and Philipson, 1971; De Sena and Mandel, 1977; Gromeier and Wetz, 1990). The myristylation of VP4 (Chow et al., 1987) induces the formation of a pore, which has been proposed to facilitate the release of viral RNA into the cytoplasm across endosomal membranes (Danthi et al., 2003).
The Arginines in the N-Terminus of the Porcine Circovirus 2 Virus-like Particles Are Responsible for Disrupting the Membranes at Neutral and Acidic pH
2019, Journal of Molecular BiologyCitation Excerpt :The FHV γ peptide requires acidification to become active, whereas the NωV γ peptide is active at neutral pH [18,19]. Binding of poliovirus to its receptor causes the capsid to undergo a conformational change to externalize the myristoylated amino acid of the VP4 capsid protein [20,21] and the amphipathic helix at N-terminus of the VP1 capsid protein [22]. Both peptides insert into and disrupt the membrane [22].
Poliovirus Receptor: More than a simple viral receptor
2017, Virus ResearchCitation Excerpt :Thus, the more LPS producing bacteria present in the GI tract, the more susceptible a host is to poliovirus infection (Kuss et al., 2011). Poliovirus initially exists in a collapsed form (160S) in the extracellular fluid (De Sena and Mandel, 1977; Tsang et al., 2001). This collapsed form of the virus depends on the presence of a hydrophobic protein core in the VP1 subunit called the pocket factor (Filman et al., 1989).
A novel multiplex poliovirus binding inhibition assay applicable for large serosurveillance and vaccine studies, without the use of live poliovirus
2017, Journal of Virological MethodsCitation Excerpt :In addition, small differences in immunogenicity between the PV strains used in both assays (Sabin vs inactivated Salk) introduced by formalin inactivation of wildtype PV contributes to this difference. Formalin inactivation not only inhibits the formation of the conformationally different PV intermediates necessary for cell infection (De Sena and Mandel, 1977; Fricks and Hogle, 1990; Twomey et al., 1995; Wilton et al., 2014; Curry et al., 1996), by cross linking the RNA to the viral capsid, but it also introduces small changes in immunogenicity, particularly in antigenic site 1 (Rezapkin et al., 2005; Chen et al., 2013; De Sena and Mandel, 1977; Twomey et al., 1995; Wilton et al., 2014; Tano et al., 2007; Ferguson et al., 1993). Antigenic site 1 is the immunodominant site for PV type 2 and one of the immunodominant sites in PV type 3, but not in PV type 1 (Herremans et al., 2000; Patel et al., 1993; Minor et al., 1986).
Viral weapons of membrane destruction: Variable modes of membrane penetration by non-enveloped viruses
2011, Current Opinion in VirologyCitation Excerpt :The poliovirus receptor (PVR/CD155) binds within the ‘canyon’ region, a depression surrounding the five-fold axis of the virus particle [16]. Binding results in the conversion of mature virions to A (135S) particles, characterized by externalization of the N-terminus of VP1 and release of VP4, both of which play a role in membrane penetration [17–20]. Following receptor binding, NEVs are frequently transported into the endolysosomal pathway.
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Present address: Department of Microbiology and Biochemistry, Idaho State University, Pocatello, Idaho 83209.