AAAR 31st Annual Conference
October 8-12, 2012
Hyatt Regency Minneapolis
Minneapolis, Minnesota, USA
Abstract View
Investigation of Possible Structural Modifications of Proteins and a Common Cold Virus at Elevated Temperature in the Gas-phase with DMA-technique
PETER KALLINGER, Victor Weiss, Dieter Blaas, Günter Allmaier, Wladyslaw Szymanski, University of Vienna
Abstract Number: 105 Working Group: Health Related Aerosols
Abstract During the last decade, the GEMMA technique (Gas-phase Electrophoretic Molecular Mobility Analyzer, a combination of a nano electrospray, DMA, and a particle detector) has proven useful for detection and size-determination of intact viruses. Human rhinoviruses (HRVs) are members of the picornavirus family and the main cause of the common cold. They are nearly spherical of icosahedral shape with a diameter of about 30 nm. On incubation at T > 50 °C, the infectious virus loses its innermost capsid protein VP4 together with its single stranded RNA genome; the resulting subviral particle is about 4% bigger than the native virion. It has been shown previously with GEMMA that subviral particles obtained on incubation at elevated temperature exhibit a change of the size spectrum with respect to the size spectrum of native virions; subviral particles, together with oligomers of the VP4 capsid protein, were detected. In order to investigate these conformational modifications online under the influence of heat, we have now used a different approach, namely heating the virus in the gas-phase. We constructed a device that can be operated at atmospheric pressure at predetermined temperature and humidity. It was integrated in the GEMMA system between the nano electrospray and the charge conditioning device in front of the DMA. Since changes of size and conformation of a given virus occur at characteristic temperatures, this apparatus might become useful for the fast online detection and study of thermal stability of viruses and other bio-nanoparticles. We shall present first results on heat-induced conformational modifications of the HRV2 capsid in the gas-phase and compare it with results of experiments carried out in solution.