Cutting edge: SR-PSOX/CXC chemokine ligand 16 mediates bacterial phagocytosis by APCs through its chemokine domain

被引：137

作者：

Shimaoka, T

Nakayama, T

Kume, N

Takahashi, S

Yamaguchi, J

Minami, M

Hayashida, K

Kita, T

Ohsumi, J

Yoshie, O

Yonehara, S

机构：

[1] Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068507, Japan

[2] Kyoto Univ, Inst Virus Res, Sakyo Ku, Kyoto 6068507, Japan

[3] Kyoto Univ, Dept Cardiovasc Med, Sakyo Ku, Grad Sch Med, Kyoto 6068507, Japan

[4] Kinki Univ, Sch Med, Dept Microbiol, Sayama, Osaka 589, Japan

[5] Biomed Res Labs, Shinagawa Ku, Tokyo, Japan

[6] Mol Biol Res Labs, Shinagawa Ku, Tokyo, Japan

来源：

JOURNAL OF IMMUNOLOGY | 2003年 / 171卷 / 04期

关键词：

D O I：

10.4049/jimmunol.171.4.1647

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 [免疫学];

摘要：

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, signficantly 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-PSOXICXCL16 may play an important role in facilitating uptake of various pathogens and chemotaxis of T and NKT cells by APCs through its chemokine domain.

引用

页码：1647 / 1651

页数：5

共 21 条

[1]

A new class of membrane-bound chemokine with a CX(3)C motif [J].