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33
A novel cell entry pathway for a DAF-using human enterovirus is dependent on lipid rafts
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, 2002
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2001. Kinetic analysis of the effect of poliovirus receptor on viral uncoating: the receptor as a catalyst
- J
"... We examined the role of soluble poliovirus receptor on the transition of native poliovirus (160S or N particle) to an infectious intermediate (135S or A particle). The viral receptor behaves as a classic transition state theory catalyst, facilitating the N-to-A conversion by lowering the activation ..."
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We examined the role of soluble poliovirus receptor on the transition of native poliovirus (160S or N particle) to an infectious intermediate (135S or A particle). The viral receptor behaves as a classic transition state theory catalyst, facilitating the N-to-A conversion by lowering the activation energy for the process by 50 kcal/mol. In contrast to earlier studies which demonstrated that capsid-binding drugs inhibit thermally mediated N-to-A conversion through entropic stabilization alone, capsid-binding drugs are shown to inhibit receptor-mediated N-to-A conversion through a combination of enthalpic and entropic effects. Poliovirus is a nonenveloped virus of the family Picornaviri-dae. Picornaviruses share an icosahedral capsid architecture consisting of 60 copies of four proteins, VP1, VP2, VP3, and VP4. The surface of the virion is dominated by prominent star-shaped mesas at the fivefold axes and three-bladed pro-peller-like features at the threefold axes. These surface fea-tures are separated by deep canyons encircling the fivefold axes. These canyons are involved in many essential aspects of capsid function. Structural studies have shown that the recep-
Interaction of coxsackievirus A21 with its cellular receptor, ICAM-1
- J Virol
, 2001
"... Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses the same cellular receptor, intercellular adhesion molecule 1 (ICAM-1), as does the major group of HRVs; unlike HRVs, however, it is stable at acid pH. The cryoelectron microscopy (cryoEM) im ..."
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Cited by 18 (2 self)
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Coxsackievirus A21 (CAV21), like human rhinoviruses (HRVs), is a causative agent of the common cold. It uses the same cellular receptor, intercellular adhesion molecule 1 (ICAM-1), as does the major group of HRVs; unlike HRVs, however, it is stable at acid pH. The cryoelectron microscopy (cryoEM) image reconstruction of CAV21 is consistent with the highly homologous crystal structure of poliovirus 1; like other enteroviruses and HRVs, CAV21 has a canyon-like depression around each of the 12 fivefold vertices. A cryoEM reconstruction of CAV21 complexed with ICAM-1 shows all five domains of the extracellular component of ICAM-1. The known atomic structure of the ICAM-1 amino-terminal domains D1 and D2 has been fitted into the cryoEM density of the complex. The site of ICAM-1 binding within the canyon of CAV21 overlaps the site of receptor recognition utilized by rhinoviruses and polioviruses. Interactions within this common region may be essential for triggering viral destabilization after attachment to susceptible cells. Enteroviruses, parechoviruses, and human rhinoviruses (HRVs) are closely related viruses belonging to the family Picornaviridae. Based on genome organization and RNA sequences, the genera Rhinovirus and Enterovirus are more closely related to each other than to the rest of the picornaviruses
Interactions of foot-and-mouth disease virus with soluble bovine V3 and V6
, 2004
"... At least four members of the integrin family of receptors, V1, V3, V6, and V8, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. Our investigators have recently shown that the efficiency of receptor usage appears to be related to the viral serotype and may be influe ..."
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Cited by 16 (5 self)
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At least four members of the integrin family of receptors, V1, V3, V6, and V8, have been identified as receptors for foot-and-mouth disease virus (FMDV) in vitro. Our investigators have recently shown that the efficiency of receptor usage appears to be related to the viral serotype and may be influenced by structural differences on the viral surface (H. Duque and B. Baxt, J. Virol. 77:2500-2511, 2003). To further examine these differences, we generated soluble V3 and V6 integrins. cDNA plasmids encoding the individual complete integrin V, 3, and 6 subunits were used to amplify sequences encoding the subunits ’ signal peptide and ectodomain, resulting in subunits lacking transmembrane and cytoplasmic domains. COS-1 cells were trans-fected with plasmids encoding the soluble V subunit and either the soluble 3 or 6 subunit and labeled with [35S]methionine-cysteine. Complete subunit heterodimeric integrins were secreted into the medium, as deter-mined by radioimmunoprecipitation with specific monoclonal and polyclonal antibodies. For the examination of the integrins ’ biological activities, stable cell lines producing the soluble integrins were generated in HEK 293A cells. In the presence of divalent cations, soluble V6 bound to representatives of type A or O viruses, immobilized on plastic dishes, and significantly inhibited viral replication, as determined by plaque reduction assays. In contrast, soluble V3 was unable to bind to immobilized virus of either serotype; however, virus bound to the immobilized integrin, suggesting that FMDV binding to V3 is a low-affinity interaction. In
Complexes of poliovirus serotypes with their common cellular receptor, CD155
- Journal of Virology
, 2003
"... Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon ..."
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Cited by 12 (1 self)
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Structures of all three poliovirus (PV) serotypes (PV1, PV2, and PV3) complexed with their cellular receptor, PV receptor (PVR or CD155), were determined by cryoelectron microscopy. Both glycosylated and fully deglycosylated CD155 exhibited similar binding sites and orientations in the viral canyon for all three PV serotypes, showing that all three serotypes use a common mechanism for cell entry. Difference maps between the glycosylated and deglycosylated CD155 complexes determined the sites of the carbohydrate moieties that, in turn, helped to verify the position of the receptor relative to the viral surface. The proximity of the CD155 carbohydrate site at Asn105 to the viral surface in the receptor-virus complex suggests that it might interfere with receptor docking, an observation consistent with the properties of mutant CD155. The footprints of CD155 on PV surfaces indicate that the south rim of the canyon dominates the virus-receptor interactions and may correspond to the initial CD155 binding state of the receptor-mediated viral uncoating. In contrast, the interaction of CD155 with the north rim of the canyon, especially the region immediately outside the viral hydrophobic pocket that normally binds a cellular “pocket factor, ” may be critical for the release of the pocket factor, decreasing the virus stability and hence initiating uncoating. The large area of the CD155 footprint on the PV surface, in comparison with other picornavirus-receptor interactions, could be a potential limitation on the viability of PV escape mutants from antibody neutralization. Many of these are likely to have lost their
Early Events in Integrin �v�6-Mediated Cell Entry of Foot-and-Mouth Disease Virus
, 2004
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Cited by 7 (3 self)
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This article cites 83 articles, 52 of which can be accessed free
Receptor Priming of Major Group Human Rhinoviruses for Uncoating and Entry at Mild Low-pH Environments
, 2003
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Cited by 2 (0 self)
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These include: This article cites 23 articles, 15 of which can be accessed free at:
Poliovirus RNA is released from the capsid near a twofold symmetry axis
- Journal of Virology
, 2011
"... After recognizing and binding to its host cell, poliovirus (like other nonenveloped viruses) faces the challenge of translocating its genome across a cellular membrane and into the cytoplasm. To avoid entanglement with the capsid, the RNA must exit via a single site on the virion surface. However, t ..."
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Cited by 2 (0 self)
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After recognizing and binding to its host cell, poliovirus (like other nonenveloped viruses) faces the challenge of translocating its genome across a cellular membrane and into the cytoplasm. To avoid entanglement with the capsid, the RNA must exit via a single site on the virion surface. However, the mechanism by which a single site is selected (from among 60 equivalents) is unknown; and until now, even its location on the virion surface has been controversial. To help to elucidate the mechanism of infection, we have used single-particle cryo-electron microscopy and tomography to reconstruct conformationally altered intermediates that are formed by the poliovirion at various stages of the poliovirus infection process. Recently, we reported icosahedrally symmetric structures for two forms of the end-state 80S empty capsid particle. Surprisingly, RNA was frequently visible near the capsid; and in a subset of the virions, RNA was seen on both the inside and outside of the capsid, caught in the act of exiting. To visualize RNA exiting, we have now determined asymmetric reconstructions from that subset, using both single-particle cryo-electron microscopy and cryo-electron tomo-graphic methods, producing independent reconstructions at 50-Å resolution. Contrary to predictions in the literature, the footprint of RNA on the capsid surface is located close to a viral 2-fold axis, covering a slot-shaped area of reduced density that is present in both of the symmetrized 80S reconstructions and which extends by about 20 Å away from the 2-fold axis toward each neighboring 5-fold axis.
Correspondence
, 2011
"... Antigenic modules in the N-terminal S1 region of the transmissible gastroenteritis virus spike protein ..."
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Antigenic modules in the N-terminal S1 region of the transmissible gastroenteritis virus spike protein
SEE PROFILE
, 2004
"... All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately. ..."
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All in-text references underlined in blue are linked to publications on ResearchGate, letting you access and read them immediately.
