Molecular Characterization and Functional Analysis of a C-type Lectin Isolated from Mosquito Armigeres subalbatus

碩士 === 國立陽明大學 === 熱帶醫學研究所 === 96 === After microorganisms have entered insect hemoceols, they are recognized by pattern recognition receptors (PRRs). Then, PRRs trigger a series of humoral and cellular immune responses against invading pathogens. Lectins, which function as PRRs, are sugar binding pr...

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Bibliographic Details
Main Authors: Hsiu-Mei Lin, 林秀美
Other Authors: Cheng-Chen Chen
Format: Others
Language:zh-TW
Published: 2008
Online Access:http://ndltd.ncl.edu.tw/handle/80185321792625377906
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Summary:碩士 === 國立陽明大學 === 熱帶醫學研究所 === 96 === After microorganisms have entered insect hemoceols, they are recognized by pattern recognition receptors (PRRs). Then, PRRs trigger a series of humoral and cellular immune responses against invading pathogens. Lectins, which function as PRRs, are sugar binding proteins that recognize specific carbohydrate structures. The first mosquito lectin, designated aslectin (AL-1), was discovered in Armigeres subalbatus. In this study, we cloned and molecular characterized the second mosquito lectin, designated aslectin2 (AL-2), from Ar. subalbatus. The 669 bp cDNA clone for AL-2 gene encodes a 174 deduced amino acid sequence that contains a calcium-dependent carbohydrate recognition domain (CRD). AL-2 is transcribed in larval, pupal and adult stages. Using AL-2 polyclonal antibody, a 17 kDa protein was detected from whole body extract of Ar. subalbatus. AL-2 protein expression was significantly enhanced following both Escherichia coli and Staphylococcus aureus challenged. These results suggested that AL-2 might function as a PRR in the immune response in Ar. subalbatus.