Journal
MOLECULAR ORAL MICROBIOLOGY
Volume 28, Issue 2, Pages 142-153Publisher
WILEY
DOI: 10.1111/omi.12011
Keywords
Aggregatibacter actinomycetemcomitans; bacterial adhesion; biofilm; human saliva; lipopolysaccharide; lipopolysaccharide-binding proteins
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Funding
- National Research Foundation (NRF) of Korea
- Ministry of Education, Science and Technology (MEST) [2009-0086835, 2011-0029827, 2011-0001030]
- Technology Development Program for Agriculture (Agriculture Research Center program)
- Ministry for Food, Agriculture, Forestry and Fisheries, Republic of Korea
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Aggregatibacter actinomycetemcomitans lipopolysaccharide (Aa.LPS) is a major virulence factor associated with aggressive periodontitis. Although the recognition of Aa.LPS is potentially initiated by salivary proteins in the oral cavity, Aa.LPS-binding proteins (Aa.LPS-BPs) in saliva are poorly characterized. The purpose of this study was to capture and identify Aa.LPS-BPs in human saliva using a LTQ-Orbitrap hybrid Fourier transform mass spectrometry. Aa.LPS conjugated onto N-hydroxysuccinimidyl-Sepharose (R) 4 Fast Flow beads (Aa.LPS-beads) activated Toll-like receptor 4 and produced nitric oxide and Interferon gamma-inducible protein-10, implying that the conjugation process did not alter the biological properties of Aa.LPS. Aa.LPS-BPs were subsequently isolated from the nine human saliva samples from healthy individuals with the Aa.LPS-beads followed by identification with the mass spectrometry. Aa.LPS-BPs include -amylase, serum albumin, cystatin, lysozyme C, submaxillary gland androgen-regulated protein 3B, immunoglobulin subunits, polymeric immunoglobulin receptor, deleted in malignant brain tumors 1, prolactin-inducible protein, lipocalin-1, and basic salivary proline-rich protein 2. Specific binding was validated using a pull-down assay with -amylase which was captured at the highest frequency. Alpha-amylase demonstrated to interfere with the adherence and biofilm formation of A.actinomycetemcomitans. Even heat-inactivated -amylase showed the interference to the same extent. Conclusively, we identified unique Aa.LPS-BPs that provide useful information to understand bacterial pathogenesis and host innate immunity in the oral cavity.
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