Human SAP Is a Novel Peptidoglycan Recognition Protein That Induces Complement-Independent Phagocytosis of <i>Staphylococcus aureus</i>

  • Jang-Hyun An
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;
  • Kenji Kurokawa
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;
  • Dong-Jun Jung
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;
  • Min-Jung Kim
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;
  • Chan-Hee Kim
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;
  • Yukari Fujimoto
    †Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan; and
  • Koichi Fukase
    †Department of Chemistry, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043, Japan; and
  • K. Mark Coggeshall
    ‡Department of Cell Biology, University of Oklahoma, Oklahoma City, OK 73104
  • Bok Luel Lee
    *Host Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 609-735, Korea;

Abstract

<jats:title>Abstract</jats:title> <jats:p>The human pathogen Staphylococcus aureus is responsible for many community-acquired and hospital-associated infections and is associated with high mortality. Concern over the emergence of multidrug-resistant strains has renewed interest in the elucidation of host mechanisms that defend against S. aureus infection. We recently demonstrated that human serum mannose-binding lectin binds to S. aureus wall teichoic acid (WTA), a cell wall glycopolymer—a discovery that prompted further screening to identify additional serum proteins that recognize S. aureus cell wall components. In this report, we incubated human serum with 10 different S. aureus mutants and determined that serum amyloid P component (SAP) bound specifically to a WTA-deficient S. aureus ΔtagO mutant, but not to tagO-complemented, WTA-expressing cells. Biochemical characterization revealed that SAP recognizes bacterial peptidoglycan as a ligand and that WTA inhibits this interaction. Although SAP binding to peptidoglycan was not observed to induce complement activation, SAP-bound ΔtagO cells were phagocytosed by human polymorphonuclear leukocytes in an FcγR-dependent manner. These results indicate that SAP functions as a host defense factor, similar to other peptidoglycan recognition proteins and nucleotide-binding oligomerization domain–like receptors.</jats:p>

Journal

  • The Journal of Immunology

    The Journal of Immunology 191 (6), 3319-3327, 2013-09-15

    The American Association of Immunologists

Citations (1)*help

See more

References(51)*help

See more

Related Projects

See more

Details 詳細情報について

Report a problem

Back to top