期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 4, 页码 2405-2414出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.528885
关键词
Integrin; Invertebrates; Phagocytosis; Protein-Protein Interactions; RNA Interference (RNAi); C-type Lectin; Opsonin
资金
- National Natural Science Foundation of China [31130056, 31302217]
- National Basic Research Program of China (973 Program) [2012CB114405]
- Ph.D. Programs Foundation of the Ministry of Education of China [20110131130003]
- Provincial Natural Science Foundation of Shandong, China [ZR2011CM014]
- China Postdoctoral Science Foundation [2013M540553]
Phagocytosis is a conserved cellular response among metazoans. Opsonins are some molecules that label targets to increase their susceptibility to phagocytosis. Opsonins are usually captured by receptors on the surface of phagocytes. Our previous study found the C-type lectin FcLec4 from Chinese white shrimp Fenneropenaeus chinensis might function as an opsonin to facilitate bacterial clearance. In the present study we purified the native FcLec4 protein and confirmed its opsonic activity in the near relation, kuruma shrimp Marsupenaeus japonicus. The possible receptor of FcLec4 was identified as -integrin by panning a T7 phage display library of shrimp hemocytes and then confirmed by co-immunoprecipitation assay. We further proved that the interaction between FcLec4 and -integrin did not rely on the carbohydrate recognition domain but on the N terminus of FcLec4. In addition, inhibition of FcLec4 expression using RNAi delayed bacterial clearance, and -integrin knockdown suppressed the opsonic activity of FcLec4. This study is the first to show the direct interaction between an opsonin and its receptor in crustaceans. Our study provides new insights into invertebrate phagocytosis and the functions of C-type lectins.
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