Abstract

Lactobacillus plantarum is a widespread probiotic bacteria found in many fermented food products. In this study, the whole-cell proteins and secretory proteins of L. plantarum were separated by two-dimensional electrophoresis method. A total of 434 proteins were identified by tandem mass spectrometry, including a plasmid-encoded hypothetical protein pLP9000_05. The information of first 20 highest abundance proteins was listed for the further genetic manipulation of L. plantarum, such as construction of high-level expressions system. Furthermore, the first interaction map of L. plantarum was established by Blue-Native/SDS-PAGE technique. A heterodimeric complex composed of maltose phosphorylase Map3 and Map2, and two homodimeric complexes composed of Map3 and Map2 respectively, were identified at the same time, indicating the important roles of these proteins. These findings provided valuable information for the further proteomic researches of L. plantarum.

Highlights

  • Lactobacillus plantarum is a kind of beneficial lactic acid bacteria (LAB) widely used by the food industries

  • Given that the genome of our strain has not been sequenced, the acquired mass spectra were initially searched against different databases generated from all of three published L. plantarum genomes

  • The results showed that number of identified proteins was larger when genome of L. plantarum JDM1 was used

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Summary

Introduction

Lactobacillus plantarum is a kind of beneficial lactic acid bacteria (LAB) widely used by the food industries now. Key proteins in the adhesion of L. plantarum, and in the response to tannic acid, bile, and alkaline stress were analyzed by proteomic methods [9,10,11,12,13]. These proteomic studies provide valuable data and pave the way for a more comprehensive insight into the molecular basis of L. plantarum. More proteins need to be identified as a reference for further proteomics research of L. plantarum, for comparative studies

Results and Discussion
Data Analysis
Materials and Methods
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