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Mass spectrometry reveals specific and global molecular transformations during viral infection.

Mass spectrometry reveals specific and global molecular transformations during viral infection. Research Abstract Details 

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  • Mass spectrometry reveals specific and global molecular transformations during viral infection. Abstract Text:

    eden p goEden P Go,william r wikoffWilliam R Wikoff,zhouxin shenZhouxin Shen,grace o'mailleGrace O'Maille,hirotoshi moritaHirotoshi Morita,thomas p conradsThomas P Conrads,anders nordstromAnders Nordstrom,sunia a traugerSunia A Trauger,wilasinee uritboonthaiWilasinee Uritboonthai,david a lucasDavid A Lucas,king c chanKing C Chan,timothy d veenstraTimothy D Veenstra,hanna lewickiHanna Lewicki,michael b oldstoneMichael B Oldstone,anette schneemannAnette Schneemann,gary siuzdakGary Siuzdak,

    Mass spectrometry analysis was used to target three different aspects of the viral infection process: the expression kinetics of viral proteins, changes in the expression levels of cellular proteins, and the changes in cellular metabolites in response to viral infection. The combination of these methods represents a new, more comprehensive approach to the study of viral infection revealing the complexity of these events within the infected cell. The proteins associated with measles virus (MV) infection of human HeLa cells were measured using a label-free approach. On the other hand, the regulation of cellular and Flock House Virus (FHV) proteins in response to FHV infection of Drosophila cells was monitored using stable isotope labeling. Three complementary techniques were used to monitor changes in viral protein expression in the cell and host protein expression. A total of 1500 host proteins was identified and quantified, of which over 200 proteins were either up- or down-regulated in response to viral infection, such as the up-regulation of the Drosophila apoptotic croquemort protein, and the down-regulation of proteins that inhibited cell death. These analyses also demonstrated the up-regulation of viral proteins functioning in replication, inhibition of RNA interference, viral assembly, and RNA encapsidation. Over 1000 unique metabolites were also observed with significant changes in over 30, such as the down-regulated cellular phospholipids possibly reflecting the initial events in cell death and viral release. Overall, the cellular transformation that occurs upon viral infection is a process involving hundreds of proteins and metabolites, many of which are structurally and functionally uncharacterized.

    Mass spectrometry reveals specific and global molecular transformations during viral infection. Publishing Authors By Initials

    ep goEP Go,wr wikoffWR Wikoff,z shenZ Shen,g o'mailleG O'Maille,h moritaH Morita,tp conradsTP Conrads,a nordstromA Nordstrom,sa traugerSA Trauger,w uritboonthaiW Uritboonthai,da lucasDA Lucas,kc chanKC Chan,td veenstraTD Veenstra,h lewickiH Lewicki,mb oldstoneMB Oldstone,a schneemannA Schneemann,g siuzdakG Siuzdak,

    For similar abstracts research abstracts see: abstracts research

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    Mass spectrometry reveals specific and global molecular transformations during viral infection. Journal Published:

    PUBLICATION TYPE: Research Support, U.S. Gov't,

    Journal: Journal of proteome research

    VOLUME: 5

    Page Numbers: 2405-16

    Journal Abbreviation:

    ISSN: 1535-3893

    DAY: 3

    MONTH: Sep

    YEAR: 2006

    Mass spectrometry reveals specific and global molecular transformations during viral infection. Information

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    LANGUAGE: eng

    NlmUniqueID: 101128775

    Mass spectrometry reveals specific and global molecular transformations during viral infection. Keywords Mesh Terms:

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    Grant and Affiliation Information for Mass spectrometry reveals specific and global molecular transformations during viral infection.

    AFFILIATION: Department of Molecular Biology and The Center for Mass Spectrometry, The Scripps Research Institute, La Jolla, California 92037, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Proteome Res

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