Public release date: 8-Mar-2011
Contact: Ellen R. Weiss
eweiss@biophysics.org
240-290-5606
American Institute of Physics
Sensitive 'PING' device described at Biophysical Meeting today in Baltimore
WASHINGTON, D.C. (March 8, 2011) -- Scientists in Israel and California have developed an instrument for rapidly analyzing molecular interactions that take place viruses and the cells they infect. By helping to identify interactions between proteins made by viruses like HIV and hepatitis and proteins made by the human cells these viruses infect, the device may help scientists develop new ways of disrupting these interactions and find new drugs for treating those infections.
According to Doron Gerber, a professor at Bar Ilan University in Ramat Gan, the PING system (Protein Interaction Network Generator) can be used to examine thousands of potential interactions at a time, and it detects them at a sensitivity 100- to 1,000-time greater than current methods. Gerber developed PING with collaborators at Stanford University, and he will describe the technology today at the 55th Annual Biophysical Society Meeting in Baltimore.
When a virus infects a human cell, it hijacks the machinery of that cell, recruiting certain host proteins and subverting them to the task of manufacturing new viral particles. This feature of viral biology has made viral infections notoriously difficult to treat, as therapies must specifically target the virus without harming the cell.
One approach that has been successful is to identify key interactions between viral and host proteins, which can then serve as targets for new drugs. For example, the HIV drug Fuzeon works by blocking a viral protein from attaching to proteins on the surface of immune system cells, barring entry to the cell. Like many antivirals, Fuzeon is used in combination with other drugs in a "cocktail." This is because, like most viruses, HIV mutates rapidly, acquiring resistance to individual drugs. Therefore, the need for new antiviral drugs is constant and ongoing.
Using PING, the Israeli and California scientists identified novel cellular partners for proteins from hepatitis C and hepatitis D. "And we can now use the same system to screen for inhibitors," says Gerber, who adds that new treatments are urgently needed for hepatitis C, for which only one treatment exists that works in only half the patient population.
Because PING employs microfluidics, very small samples can be used; gathering enough material has been a particular challenge with existing methods.
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The presentation, "Mapping Virus-Host Protein Interactions Using the PING Microfluidics Platform," is at 5:00 p.m. on Tuesday, March 8, 2011 in Room 307 of the Baltimore Convention Center. ABSTRACT: http://tinyurl.com/67lnomy
The research was funded by the NIH Pioneer grant.
MORE MEETING INFORMATION
Each year, the Biophysical Society Annual Meeting brings together more than 6,000 scientists and hosts more than 4,000 poster presentations, 200 exhibits, and more than 20 symposia. The largest meeting of its type in the world, the Biophysical Society Annual Meeting retains its small-meeting flavor through its subgroup meetings, platform sessions, social activities, and committee programs.
QUICK LINKS
Meeting Home Page: http://www.biophysics.org/2011meeting
General Meeting Information: http://www.biophysics.org/GeneralInfo/Overview/tabid/2062/Default.aspx
Search abstracts: http://www.abstractsonline.com/plan/start.aspx?mkey={FEA830A5-24AD-47F3-8E61-FCA29F5FEF34}
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ABOUT THE BIOPHYSICAL SOCIETY
The Biophysical Society, founded in 1956, is a professional, scientific society established to encourage development and dissemination of knowledge in biophysics. The society promotes growth in this expanding field through its annual meeting, monthly journal, and committee and outreach activities. Its over 9,000 members are located throughout the U.S. and the world, where they teach and conduct research in colleges, universities, laboratories, government agencies, and industry. For more information on the society or the 2011 Annual Meeting, visit http://www.biophysics.org/
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