Proteomics

Dataset Information

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Surface Proteins of Listeria monocytogenes


ABSTRACT: Listeria monocytogenes cells (strain LI0521) were digested with trypsin for the identification of surface proteins. The supernatant was filter-sterilized and subjected to identification by LC-MS/MS. Concurrently secreted or shed proteins were identified by isolating filter-sterilized supernatants following incubation of L. monocytogenes cells in buffer without trypsin. This was followed by trypsin digest of the sterilized supernatant and identification by LC-MS/MS.

INSTRUMENT(S): Synapt HDMS, MALDI Synapt HDMS

ORGANISM(S): Listeria Monocytogenes

SUBMITTER: Min Lin  

LAB HEAD: Min Lin

PROVIDER: PXD000035 | Pride | 2013-08-27

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
20111118_CZhang01.zip Other
20111118_CZhang02.zip Other
20111118_CZhang03.zip Other
20111118_CZhang04.zip Other
20111118_CZhang05.zip Other
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Publications

Proteomic identification of Listeria monocytogenes surface-associated proteins.

Zhang Cathy X Y CX   Creskey Marybeth C MC   Cyr Terry D TD   Brooks Brian B   Huang Hongsheng H   Pagotto Franco F   Lin Min M  

Proteomics 20131001 20


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 th  ...[more]

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