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Inmembrane, a bioinformatic workflow for annotation of bacterial cell-surface proteomes.


ABSTRACT: BACKGROUND:The annotation of surface exposed bacterial membrane proteins is an important step in interpretation and validation of proteomic experiments. In particular, proteins detected by cell surface protease shaving experiments can indicate exposed regions of membrane proteins that may contain antigenic determinants or constitute vaccine targets in pathogenic bacteria. RESULTS:Inmembrane is a tool to predict the membrane proteins with surface-exposed regions of polypeptide in sets of bacterial protein sequences. We have re-implemented a protocol for Gram-positive bacterial proteomes, and developed a new protocol for Gram-negative bacteria, which interface with multiple predictors of subcellular localization and membrane protein topology. Through the use of a modern scripting language, inmembrane provides an accessible code-base and extensible architecture that is amenable to modification for related sequence annotation tasks. CONCLUSIONS:Inmembrane easily integrates predictions from both local binaries and web-based queries to help gain an overview of likely surface exposed protein in a bacterial proteome. The program is hosted on the Github repository http://github.com/boscoh/inmembrane.

SUBMITTER: Perry AJ 

PROVIDER: S-EPMC3668253 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Inmembrane, a bioinformatic workflow for annotation of bacterial cell-surface proteomes.

Perry Andrew J AJ   Ho Bosco K BK  

Source code for biology and medicine 20130319 1


<h4>Background</h4>The annotation of surface exposed bacterial membrane proteins is an important step in interpretation and validation of proteomic experiments. In particular, proteins detected by cell surface protease shaving experiments can indicate exposed regions of membrane proteins that may contain antigenic determinants or constitute vaccine targets in pathogenic bacteria.<h4>Results</h4>Inmembrane is a tool to predict the membrane proteins with surface-exposed regions of polypeptide in s  ...[more]

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