Journal
MOLECULAR IMMUNOLOGY
Volume 65, Issue 1, Pages 77-85Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2015.01.007
Keywords
Peptidoglycan; Peptidoglycan-binding proteins; Lactobacillus plantarum; Staphylococcus aureus; Gastrointestinal tract
Categories
Funding
- National Research Foundation of Korea - Korean government (MISIP) [2010-0029116, 2008-0062421, NRF-2012R1A1A2039022]
- Agriculture, Food and Rural Affairs Research Center Support Program
- Ministry of Agriculture, Food and Rural Affairs
- Korea Health Industry Development Institute (KHIDI) - Ministry of Health & Welfare, Republic of Korea. [HI14C0469]
- National Research Foundation of Korea [2010-0029116, 2008-0062421] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Peptidoglycan (PGN) is a major cell wall component of Gram-positive bacteria that contributes to the regulation of host immunity in the gastrointestinal tract (GIT). Although Gram-positive bacteria contain structurally distinct PGNs that are considered to differently interact with the GIT, PGN-binding proteins (PGN-BPs) in the GIT have been poorly understood. In the present study, we purified PGNs from Lactobacillus plantarum and Staphylococcus aureus (named as Lp.PGN and Sa.PGN, respectively) and identified Lp.PGN-BPS and Sa.PGN-BPs in the lysate of mouse GIT. Lp.PGN activated nucleotide-binding oligomerization domain (NOD) 1 and NOD2, whereas Sa.PGN activated NOD2, but not NOD1, implying that both PGNs retained the biological activity and were differently recognized by the host cells. PGN-BPs were isolated by precipitation with Lp.PGN or Sa.PGN and identified using LTQ-Orbitrap hybrid Fourier transform mass spectrometry. Three independent experiments demonstrated that 18 Lp.PGN-BPs and 6 Sa.PGN-BPs were reproducibly obtained with statistical significance (P< 0.05). Both Lp.PGN and Sa.PGN bound to proteins which are related to cytoskeleton, microbial adhesion, and mucosal integrity. Lp.PGN selectively bound to proteins related to gene expression, chaperone, and antimicrobial function. However, Sa.PGN preferentially interacted with proteins involved in adherence and invasion of pathogens. Collectively, these results suggest that bacterial PGNs interact with the proteins regulating mucosal homeostasis and immunity in the gut and PGNs of commensals and pathogens might be also differentially recognized in the GIT. (C) 2015 Elsevier Ltd. All rights reserved.
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