期刊
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷 29, 期 1, 页码 43-51出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2004.06.001
关键词
apolipophorin III; Gm protein-24; antibacterial peptide; prophenoloxidase cascade; hemolymph; Galleria mellonella
Two hemolymph proteins were isolated from the wax moth, Galleria mellonella, larvae by a two-step procedure consisting of acid extraction and reversed phase (RP)-HPLC. One was an apolipophorin III (apoLp-III) previously characterized as a lipopolysaccharide (LPS) binding protein in the hemolymph of G. mellonella. The other was confirmed to be a new protein with a molecular mass of 23,768.69 Da, referred to as Gm protein-24. The full-length cDNA of Grn protein-24 was cloned from the fat body. The cDNA structure showed that it is a 219-residues protein derived from the precursor of 236 amino acids. The effects of apoLp-III and Gm protein-24 have been tested on the insect Immoral immunity. ApoLp-III enhanced the activity of antibacterial peptide such as cecropin but Gin protein-24 had no effect on cecropin activity. On the other hand, Gm protein-24 and apoLp-III were both involved in the activation of prophenoloxidase (PPO) cascade, which has been regarded as a critical immune reaction in insect hemolymph. Of note, the Gm protein-24 was a significantly stronger activator of PPO cascade than apoLp-III. (C) 2004 Elsevier Ltd. All rights reserved.
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