TY - JOUR
T1 - Tissue binding patterns and in vitro effects of campylobacter jejuni DNA-binding protein from starved cells
AU - Piao, Hua
AU - Minohara, Motozumi
AU - Kawamura, Nobutoshi
AU - Li, Wei
AU - Matsushita, Takuya
AU - Yamasaki, Ryo
AU - Mizunoe, Yoshimitsu
AU - Kira, Jun Ichi
N1 - Funding Information:
Acknowledgments This work was supported in part by grants from the Ministry of Education, Culture, Sports, Science and Technology of Japan, a Neuroimmunological Disease Research Committee grant from the Ministry of Health, Labour and Welfare of Japan and a grant for Research on Brain Science. We thank Tomo Iwashima and Magnus Hallstrom for their technical assistance.
PY - 2011/1
Y1 - 2011/1
N2 - Campylobacter jejuni (C. jejuni) is frequently associated with axonal Guillain-Barré syndrome (GBS). We reported that C. jejuni DNA-binding protein from starved cells (C-Dps) binds to and damages myelinated nerves in vivo. We studied the binding patterns of C-Dps to nervous tissues and its in vitro effects on neural cells. Immunohistochemically, C-Dps labeled the nodes of Ranvier, the outermost parts of internodal myelin and the basement membrane in the peripheral nerves, and neurons and myelin in the central nervous tissues. Its binding was blocked by sulfatide. C-Dps bound to the cell surfaces of nerve growth factor (NGF)-treated PC12 cells leading to dose-dependent LDH release, which was inhibited by either heat-denaturation of C-Dps or coincubation with an anti-C-Dps mAb. However, its binding to the surfaces of cultured NSC34 cells, S16 cells, or dorsal root ganglion cells, did not induce cytotoxicity. These findings suggest a possible involvement of C-Dps in C. jejuni-related GBS.
AB - Campylobacter jejuni (C. jejuni) is frequently associated with axonal Guillain-Barré syndrome (GBS). We reported that C. jejuni DNA-binding protein from starved cells (C-Dps) binds to and damages myelinated nerves in vivo. We studied the binding patterns of C-Dps to nervous tissues and its in vitro effects on neural cells. Immunohistochemically, C-Dps labeled the nodes of Ranvier, the outermost parts of internodal myelin and the basement membrane in the peripheral nerves, and neurons and myelin in the central nervous tissues. Its binding was blocked by sulfatide. C-Dps bound to the cell surfaces of nerve growth factor (NGF)-treated PC12 cells leading to dose-dependent LDH release, which was inhibited by either heat-denaturation of C-Dps or coincubation with an anti-C-Dps mAb. However, its binding to the surfaces of cultured NSC34 cells, S16 cells, or dorsal root ganglion cells, did not induce cytotoxicity. These findings suggest a possible involvement of C-Dps in C. jejuni-related GBS.
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U2 - 10.1007/s11064-010-0263-7
DO - 10.1007/s11064-010-0263-7
M3 - Article
C2 - 20853141
AN - SCOPUS:78651274745
SN - 0364-3190
VL - 36
SP - 58
EP - 66
JO - Neurochemical Research
JF - Neurochemical Research
IS - 1
ER -