NIH Proteomics Interest Group

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ProtIG is an NIH Special Interest Group (SIG) that organizes seminars and workshops in relevant areas of proteomics, including talks on separation and protein identification methods, determination of post-translational modifications, protein-protein interactions, and bioinformatics and data management. A monthly seminar series is usually held at 12 pm on the Second Thursday of each month (always check the Mtgs/Seminars button on this page for these and other PROTIG announced meetings). To receive email announcements of ProtIG events, join the listserv (Join the SIG button on this page)

April ProtIG Seminar
Please note the start time has been adjusted for 2021-2022 seminars
Thursday, April 14th, 2022
12:00 pm - 1:00 pm EDT
David Goodlett, Ph.D.
Professor of Biochemistry and Microbiology
Director of the Proteomic Centre
Don and Eleanor Rix BC Leadership Chair in Biomedical and Environmental Proteomics
University of Victoria


ďThe need for single and near cell mass spectrometry in biology.Ē

For the last twenty years (while not being distracted by proteomics) our laboratory has worked with the Ernst laboratory (UMB) on the structure activity relationship (SAR) of lipid A, which in mammals is recognized by Toll receptor 4 (TLR4). Lipid A serves as the membrane anchor for the much larger lipopolysaccharide (LPS) molecule in the outer membrane of most Gram negative bacteria. Interactions with TLR4 can produce a range of activities from agnostic to antagonistic that are directly related to structure (e.g. Li). Lipid A interaction with TLR4 is involved in the well known cytokine cascade that can aid the host in clearing an infection or if unchecked lead to a deadly cytokine storm or in some cases result in failure to be recognized due to structural changes. To exploit this moleculeís potential for use as vaccine adjuvants and antisepsis therapeutics (e.g. Scott) we are working to better define the SAR. Iíll use known changes to lipid A structure that occur as a function of environmental changes (e.g. Leung) and changes to proteomes in biofilms (e.g. Freiberg) to justify our need for single and near-single cell proteomics. Iíll present the above topics from the perspective of how mass spectrometry is helping to solve these problems with an emphasis on why we need to be able to characterize microbes and cancer cells directly as taken from their environments; i.e. without culture in the laboratory. That direct from specimen concept is the driving force behind our UVic laboratoryís efforts and it will also increasingly have an influence on how science is done at the UVic Proteomics Centre. Iíll described how we are approaching the task of near single cell analysis by mass spectrometry using adaptations to the microPOTS (Weke) and autoPOTS (Liang) methods as well review the UVic Proteomic Centre capabilities., which include targeted metabolomic assays and resurrection of mass spectrometry imaging.



REFERENCES Freiberg, JA et al. mSystems 2016; Li Y et al. Rapid Commun Mass Spectrom. 2016; Liang Y et al. Anal Chem 2021; Leung LM et al.. Scientific Reports, 2017; Scott AJ et al. Biochim Biophys Acta. 2017; Weke et al. J Proteome Research. 2021



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This site was updated on April 6th, 2022. Please contact Renee Olano at olanol(at)mail.nih.gov with questions or suggestions.