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A proteomic view of Bifidobacterium infantis generated by multi‐dimensional chromatography coupled with tandem mass spectrometry
Author(s) -
Vitali Beatrice,
Wasinger Valerie,
Brigidi Patrizia,
Guilhaus Michael
Publication year - 2005
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200401080
Subject(s) - proteome , proteomics , tandem mass spectrometry , isoelectric point , isobaric labeling , biology , computational biology , tandem mass tag , mass spectrometry , peptide mass fingerprinting , bifidobacterium longum , biochemistry , isoelectric focusing , genome , two dimensional gel electrophoresis , bifidobacterium , chemistry , chromatography , protein mass spectrometry , quantitative proteomics , enzyme , lactobacillus , fermentation , gene
Bifidobacteria are Gram‐positive prokaryotes that naturally colonize the human gut where they exert several health‐promoting effects. The present paper reports the use of a strong cation exchange‐reversed‐phase‐tandem mass spectrometry strategy to catalogue the most abundantly expressed proteins of a probiotic Bifidobacterium infantis strain. A global view of the B. infantis proteome was obtained. The bimodal representation of the proteins identified by mass spectrometry provides the first theoretical two‐dimensional map of protein distribution for this organism. Among the 136 proteins identified by multidimensional protein identification technology (MudPIT) analysis, 118 showed the highest similarity with the translated sequences of B. longum genome, two proteins were similar to other Bifidobacterium species and the remaining 16 were similar to different genera. Specific biological activities have been assigned to 115 identified proteins, whereas 21 have been referred to the group of hypothetical proteins. The MudPIT approach allowed us to identify high mass and basic isoelectric point proteins that are generally challenging to visualize using the traditional two‐dimensional electrophoresis technique. Redundancy in peptide and protein identification using the double chromatography technique was also evaluated.