TY - JOUR
T1 - Identification and gene expression of bovine C-type lectin dectin-2
AU - Bonkobara, M.
AU - Hoshino, M.
AU - Yagihara, H.
AU - Tamura, K.
AU - Isotani, M.
AU - Tanaka, Y.
AU - Washizu, T.
AU - Ariizumi, K.
N1 - Funding Information:
This research was supported partially by a Grant-in-Aid for Scientific Research (No. 16780214) and “High-Tech Research Center” Project for Private Universities: matching fund subsidy (2004–2008) from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
PY - 2006/3/15
Y1 - 2006/3/15
N2 - The C-type lectin receptor has been shown to recognize carbohydrate moieties of self and non-self antigens, thus serving as an innate immune receptor. Using bioinformatics and molecular cloning techniques, we isolated a bovine gene that encodes a polypeptide of 206 amino acids with structural features shared by mouse and human dectin-2, including a high homology with mouse dectin-2 (66%), a type II configuration, a short cytoplasmic domain without tyrosine-based signal motifs, a carbohydrate recognition domain, a putative N-glycosylation site, and an EPN motif involved in the Ca 2+-dependent binding of hexose carbohydrates. These results reveal this bovine gene to be a counterpart of mouse dectin-2. Moreover, the bovine dectin-2 gene showed heterogeneity in mRNA (the generation of alternatively spliced transcript) and segmentation into six exons, which are also observed in mouse dectin-2. Inconsistent with mouse dectin-2 mRNA, the bovine counterpart is abundantly expressed by Langerhans cells compared to macrophages; however, lymph nodes showed the highest expression level of bovine dectin-2, while spleen and lung showed the highest expression levels of mouse and human dectin-2. In cattle, dectin-2 expressed by dendritic cells may be clinically involved in the recognition of invading antigens in lymph nodes.
AB - The C-type lectin receptor has been shown to recognize carbohydrate moieties of self and non-self antigens, thus serving as an innate immune receptor. Using bioinformatics and molecular cloning techniques, we isolated a bovine gene that encodes a polypeptide of 206 amino acids with structural features shared by mouse and human dectin-2, including a high homology with mouse dectin-2 (66%), a type II configuration, a short cytoplasmic domain without tyrosine-based signal motifs, a carbohydrate recognition domain, a putative N-glycosylation site, and an EPN motif involved in the Ca 2+-dependent binding of hexose carbohydrates. These results reveal this bovine gene to be a counterpart of mouse dectin-2. Moreover, the bovine dectin-2 gene showed heterogeneity in mRNA (the generation of alternatively spliced transcript) and segmentation into six exons, which are also observed in mouse dectin-2. Inconsistent with mouse dectin-2 mRNA, the bovine counterpart is abundantly expressed by Langerhans cells compared to macrophages; however, lymph nodes showed the highest expression level of bovine dectin-2, while spleen and lung showed the highest expression levels of mouse and human dectin-2. In cattle, dectin-2 expressed by dendritic cells may be clinically involved in the recognition of invading antigens in lymph nodes.
KW - Bovine
KW - C-type lectin receptor
KW - Cloning
KW - Dectin-2
KW - Langerhans/dendritic cell
UR - http://www.scopus.com/inward/record.url?scp=32044452198&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=32044452198&partnerID=8YFLogxK
U2 - 10.1016/j.vetimm.2005.08.031
DO - 10.1016/j.vetimm.2005.08.031
M3 - Article
C2 - 16213030
AN - SCOPUS:32044452198
SN - 0165-2427
VL - 110
SP - 179
EP - 186
JO - Veterinary Immunology and Immunopathology
JF - Veterinary Immunology and Immunopathology
IS - 1-2
ER -