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Muramyl dipeptide potentiates staphylococcal lipoteichoic acid induction of cyclooxygenase-2 expression in macrophages

Authors
  • Ahn, Ki Bum
  • Jeon, Jun Ho
  • Baik, Jung Eun
  • Park, Ok-Jin
  • Kang, Seok-Seong
  • Yun, Cheol-Heui
  • Park, Jong-Hwan
  • Han, Seung Hyun1, 2, 3, 4, 5, 6, 7, 8, 9, 5, 10, 11, 12
  • 1 Department of Oral Microbiology and Immunology
  • 2 DRI
  • 3 BK21 Plus Program
  • 4 School of Dentistry
  • 5 Seoul National University
  • 6 Division of High-risk Pathogen Research
  • 7 Center for Infectious Diseases
  • 8 Korean National Institute of Health
  • 9 Department of Agricultural Biotechnology and Research Institute for Agriculture and Life Sciences
  • 10 Department of Biochemistry
  • 11 College of Medicine
  • 12 Konyang University
Type
Published Article
Journal
Microbes and Infection
Publisher
Elsevier
Publication Date
Jan 01, 2013
Accepted Date
Oct 25, 2013
Volume
16
Issue
2
Pages
153–160
Identifiers
DOI: 10.1016/j.micinf.2013.10.018
Source
Elsevier
Keywords
License
Unknown

Abstract

Gram-positive bacteria contain lipoteichoic acid (LTA) and peptidoglycan (PGN) layers, both of which are considered as major virulence factors associated with inflammation. Cyclooxygenase-2 (COX-2) plays an important role in the inflammation by generating prostaglandins at infections. Since LTA and PGN are thought to cooperate in the establishment of inflammation, we examined the ability of staphylococcal LTA (Sa.LTA) to induce COX-2 expression in the presence of muramyl dipeptide (MDP), which is the minimal structural unit of PGN required for inflammation, in macrophages. While MDP failed to induce COX-2 expression, Sa.LTA alone was sufficient to induce COX-2 production. Treatment with MDP enhanced Sa.LTA-induced COX-2 and prostaglandin E2 production. The cooperative effect between Sa.LTA and MDP was not observed in COX-2 expression by macrophages derived from Toll-like receptor 2 (TLR2)- or nucleotide-binding oligomerization domain 2 (NOD2)-deficient mice. In addition, MDP enhanced Sa.LTA-induced activation of the transcription factors NF-κB and CRE, which are known to modulate COX-2 gene transcription. Conclusively, these results suggest that MDP and Sa.LTA cooperatively induce inflammatory response by overproducing COX-2 through NOD2 and TLR2.

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