Cutting Edge: SR-PSOX/CXC Chemokine Ligand 16 Mediates Bacterial Phagocytosis by APCs Through its Chemokine Domain
Author(s) -
Takeshi Shimaoka,
Takashi Nakayama,
Noriaki Kume,
Shu Takahashi,
Junko Yamaguchi,
Manabu Minami,
Kazutaka Hayashida,
Toru Kita,
Jun Ohsumi,
Osamu Yoshie,
Shin Yonehara
Publication year - 2003
Publication title -
the journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.737
H-Index - 372
eISSN - 1550-6606
pISSN - 0022-1767
DOI - 10.4049/jimmunol.171.4.1647
Subject(s) - cxcl16 , xcl2 , chemotaxis , ccl25 , chemokine , scavenger receptor , cxc chemokine receptors , microbiology and biotechnology , phagocytosis , cxcl2 , c c chemokine receptor type 6 , ccl21 , cc chemokine receptors , cxcl9 , chemokine receptor , chemistry , biology , receptor , immunology , inflammation , biochemistry , lipoprotein , cholesterol
SR-PSOX and CXC chemokine ligand (CXCL)16, which were originally identified as a scavenger receptor and a transmembrane-type chemokine, respectively, are indicated to be identical. In this study, we demonstrate that membrane-bound SR-PSOX/CXCL16 mediates adhesion and phagocytosis of both Gram-negative and Gram-positive bacteria. Importantly, our prepared anti-SR-PSOX mAb, which suppressed chemotactic activity of SR-PSOX, significantly inhibited bacterial phagocytosis by human APCs including dendritic cells. Various scavenger receptor ligands inhibited the bacterial phagocytosis of SR-PSOX. In addition, the recognition specificity for bacteria was determined by only the chemokine domain of SR-PSOX/CXCL16. Thus, SR-PSOX/CXCL16 may play an important role in facilitating uptake of various pathogens and chemotaxis of T and NKT cells by APCs through its chemokine domain.
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