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Looking for the most current news, updates, and articles relating to microbiology, go to The American Society for Microbiology educational website Microbe World. Antiviral therapeutics play a key role in clinical management of viral diseases and protecting public health. Poliovirus (PV) is an excellent candidate for studying the molecular mechanisms of viral infection in atomic detail, both because PV is one of the most well-studied animal viruses and its infection process is representative of many other non-enveloped viruses, such as rotavirus, adenovirus, and polyomavirus. Raising your credit score can lead to savings of hundreds of thousands of dollars over the life of a mortgage. We educate you every step of the way so you know how you can continue to manage your credit long after your time with Credit Strategies.
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Effectiveness of antiviral drug treatments is continually challenged by emergence of drug-resistant viral strains.


Although PV has been extensively characterized by biochemical, genetic, cell-biological, and structural methods, the molecular details of the infection mechanism are unknown. Previous work by the Center, as well as other groups, has demonstrated that molecular dynamics (MD) can successfully describe the structure and dynamics of virus particles. In addition, a higher credit score can help you with credit card rates, auto loans, and help you get that job you wanted.
The urgency of developing new antiviral drugs has been demonstrated by obsolescence of amantadine for influenza treatment, as well as the 2009 pandemic outbreak of swine flu.
Many viruses have been visualized, sometimes at near-atomic resolution, by cryo-electron microscopy (cryo-EM) 3-D reconstruction. Therefore, identification of novel targets for development of antiviral drugs is an ongoing biomedical necessity.
Cryo-electron tomography has also provided lower resolution structures of single virus particles in complex with membranes during the infection process. In the context of PV infection, there are high-resolution reconstructions of three cell entry intermediate states. VP1 and VP4 associate with the membrane to form the VP1-VP4-membrane complex, which is shown as a cartoon.
The first state, 160S-PVR, is the virus bound to poliovirus receptor (PVR) on the cell surface.


The development of drugs targeting virus cell entry requires atomically detailed information on the molecular mechanisms underlying viral infection. The externalized VP1 N-terminus is believed to form an amphipathic helix that anchors the 135S particle to the cell surface.
Membrane associated VP4 is involved in translocation of the viral genome into the cytoplasm of the cell. There is a structural transition from the 160S to the 135S state, involving externalization of hydrophobic viral proteins (VP), the VP1 N-terminus and VP4, needed for membrane anchoring and RNA translocation across the membrane. The last is the 80S state, which is PV in the process of RNA release and membrane penetration. The RNA genome is released from the 80S particle and the 80S-membrane complex translocates the viral RNA across the membrane.



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