TY - JOUR
T1 - C-type lectin receptors dectin-3 and dectin-2 form a heterodimeric pattern-recognition receptor for host defense against fungal infection
AU - Zhu, Le Le
AU - Zhao, Xue Qiang
AU - Jiang, Changying
AU - You, Yun
AU - Chen, Xiao Ping
AU - Jiang, Yuan Ying
AU - Jia, Xin Ming
AU - Lin, Xin
N1 - Funding Information:
This work was supported by The Shanghai Basic Research Program (12JC1408401; X.-M.J), The National Basic Research Program of China (Program 973, 2013CB531602; Y.-Y.J.), NIH grants AI050848 and GM065899 (X.L.), and a Lecture Professorship Fund from Tongji University (X.L.).
PY - 2013/8/22
Y1 - 2013/8/22
N2 - C-type lectin receptors (CLRs) play critical roles as pattern-recognition receptors (PRRs) for sensing Candida albicans infection, which can be life-threatening for immunocompromised individuals. Here wehave shown that Dectin-3 (also called CLECSF8, MCL, or Clec4d), a previously uncharacterized CLR,recognized α-mannans on the surfaces of C.albicans hyphae and induced NF-κB activation. Mice with either blockade or genetically deleted Dectin-3 were highly susceptible to C.albicans infection. Dectin-3 constantly formed heterodimers with Dectin-2, a well-characterized CLR, for recognizing C.albicans hyphae. Compared to their respective homodimers, Dectin-3 and Dectin-2 heterodimers bound α-mannans more effectively, leading to potent inflammatory responses against fungal infections. Together, our study demonstrates that Dectin-3 forms a heterodimeric PRR with Dectin-2 for sensing fungal infection and suggests that different CLRs may form different hetero- and homodimers, which provide different sensitivity and diversity for host cells to detect various microbial infections.
AB - C-type lectin receptors (CLRs) play critical roles as pattern-recognition receptors (PRRs) for sensing Candida albicans infection, which can be life-threatening for immunocompromised individuals. Here wehave shown that Dectin-3 (also called CLECSF8, MCL, or Clec4d), a previously uncharacterized CLR,recognized α-mannans on the surfaces of C.albicans hyphae and induced NF-κB activation. Mice with either blockade or genetically deleted Dectin-3 were highly susceptible to C.albicans infection. Dectin-3 constantly formed heterodimers with Dectin-2, a well-characterized CLR, for recognizing C.albicans hyphae. Compared to their respective homodimers, Dectin-3 and Dectin-2 heterodimers bound α-mannans more effectively, leading to potent inflammatory responses against fungal infections. Together, our study demonstrates that Dectin-3 forms a heterodimeric PRR with Dectin-2 for sensing fungal infection and suggests that different CLRs may form different hetero- and homodimers, which provide different sensitivity and diversity for host cells to detect various microbial infections.
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U2 - 10.1016/j.immuni.2013.05.017
DO - 10.1016/j.immuni.2013.05.017
M3 - Article
C2 - 23911656
AN - SCOPUS:84882714745
SN - 1074-7613
VL - 39
SP - 324
EP - 334
JO - Immunity
JF - Immunity
IS - 2
ER -