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Current Pharmaceutical Biotechnology

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ISSN (Print): 1389-2010
ISSN (Online): 1873-4316

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Research Article

e-Membranome: A Database for Genome-Wide Analysis of Escherichia coli Outer Membrane Proteins

Author(s): Kang M. Lee, Cheorl-Ho Kim, Jong H. Kim, Sung S. Kim and Seung-Hak Cho*

Volume 22, Issue 4, 2021

Published on: 10 June, 2020

Page: [501 - 507] Pages: 7

DOI: 10.2174/1389201021666200610105549

Price: $65

Abstract

Objective: Lectin-like adhesins of enteric bacterial pathogens such as Escherichia coli are an attractive target for vaccine or drug development. Here, we have developed e-Membranome as a database of genome-wide putative adhesins in Escherichia coli (E. coli).

Methods: The outer membrane adhesins were predicted from the annotated genes of Escherichia coli strains using the PSORTb program. Further analysis was performed using Interproscan and the String database. The candidate proteins can be investigated for homology modeling of the Three-Dimensional (3D) structure (I-TASSER version 5.1), epitope region (ABCpred), and the glycan array.

Results: e-Membranome is implemented using the Django (version 2.2.5) framework. The Web Application Server Apache Tomcat 6.0 is integrated into the platform on Ubuntu Linux (version 16.04). MySQL database (version 5.7) is used as a database engine. The information on homology model of the 3D structure, epitope region, and affinity information from the glycan array will be stored in the e- Membranome database. As a case study, we performed a genome-wide screening of outer membraneembedded proteins from the annotated genes of E. coli using the e-Membranome pipeline.

Conclusion: This platform is expected to be a valuable resource for advancing research of outer membrane proteins for the construction of lectin-glycan interaction network of E. coli. In addition, the e- Membranome pipeline can be extended to other similar biological systems that need to address hostpathogen interactions.

Keywords: Escherichia coli, outer membrane-embedded proteins, genome-wide screening, e-Membranome, lectin-glycan interaction, lectin-like adhesins.

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