investigating the effect of growth phase on the surface-layer associated proteome of lactobacillus acidophilus using quantitative proteomics
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2017
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Abstract
Bacterial surface-layers (S-layers) are semi-porous crystalline arrays that self-assemble to form the outermost layer of some cell envelopes. S-layers have been shown to act as scaffolding structures for the display of auxiliary proteins externally. These S-layer associated proteins have recently gained attention in probiotics due to their direct physical contact with the intestinal mucosa and potential role in cell proliferation, adhesion, and immunomodulation. A number of studies have attempted to catalog the S-layer associated proteome of Lactobacillus acidophilus NCFM under a single condition. However, due to the versatility of the cell surface, we chose to employ a multiplexing-based approach with the intention of accurately contrasting multiple conditions. In this study, a previously described lithium chloride isolation protocol was used to release proteins bound to the L. acidophilus S-layer during logarithmic and early stationary growth phases. Protein quantification values were obtained via TMT (tandem mass tag) labeling combined with a triple-stage mass spectrometry (MS3) method. Results showed significant growth stage-dependent alterations to the surface-associated proteome while simultaneously highlighting the sensitivity and reproducibility of the technology. Thus, this study establishes a framework for quantifying condition-dependent changes to cell surface proteins that can easily be applied to other S-layer forming bacteria.
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klotz2017frontiersinvestigating
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| Authors | ;Courtney Klotz;Courtney Klotz;Sarah O'Flaherty;Yong Jun Goh;Rodolphe Barrangou;Rodolphe Barrangou |
| Journal | journal of magnetic resonance (san diego, calif : 1997) |
| Year | 2017 |
| DOI |
10.3389/fmicb.2017.02174
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