Proteomic identification of Listeria monocytogenes surface‐associated proteins |
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| Authors: | Cathy X Y Zhang Marybeth C Creskey Terry D Cyr Brian Brooks Hongsheng Huang Franco Pagotto Min Lin |
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| Institution: | 1. Ottawa Laboratory Fallowfield, Canadian Food Inspection Agency, , Ottawa, ON, Canada;2. Department of Biochemistry, Microbiology and Immunology, University of Ottawa, , Ottawa, ON,, Canada;3. Centre for Vaccine Evaluation, Health Canada, , Ottawa, ON, Canada;4. Listeriosis Reference Service, Bureau of Microbial Hazards, Health Canada, , Ottawa, ON, Canada |
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| Abstract: | This study aimed to identify proteins exposed on the surface of Listeria monocytogenes cells for diagnostic reagent development. Brief trypsin treatment of L. monocytogenes cells followed by peptide separation and identification by nano‐LC and online‐MS/MS was performed. In parallel, as a negative control, proteins secreted into the digest buffer as well as proteins from cell lysis were identified. One hundred and seventy‐four proteins were identified in at least two of three trials in either the negative control or during cell digest. Nineteen surface, 21 extracellularly secreted, 132 cytoplasmic, and two phage proteins were identified. Immunofluorescence microscopy of L. monocytogenes cells revealed the surface localization of two potential candidates for L. monocytogenes isolation and detection: lipoprotein LMOf2365_0546 and PBPD1 (LMOf2365_2742). In this report, we present the first data set of surface‐exposed L. monocytogenes proteins currently available. The data have been deposited to the ProteomeXchange Consortium with identifier PXD000035. |
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| Keywords: | Listeria monocytogenes Microbiology Protein digest Protein identification |
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