Open Access

ARTICLE

Molecular cloning and characterization of a novel mannosebinding lectin cDNA from Zantedeschia aethiopica

by ZHONGHAI CHEN, YONGZHEN PANG, XIAOJUN LIU, XINGLONG WANG, ZHONGXIANG DENG, XIAOFEN SUN, KEXUAN TANG

1. State Key Laboratory of Genetic Engineering, School of Life Sciences, Morgan-Tan International Center for Life Sciences, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Fudan University, Shanghai 200433, People’s Republic of China.
2. Plant Biotechnology Research Center, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, School of Agriculture and Biology, Shanghai Jiaotong University, Shanghai 200030, People’s Republic of China.
Address correspondence to: Kexuan Tang / Xiaofen Sun. State Key Laboratory of Genetic Engineering, School of Life Sciences, Fudan University, Shanghai 200433, PEOPLE’S REPUBLIC OF CHINA. Tel: +86-21-65642772, Fax: +86-21-65643552, Email: kxtang1@yahoo.com or kxtang1@sohu.com or xfsun1@sohu.com

BIOCELL 2005, 29(2), 187-193. https://doi.org/10.32604/biocell.2005.29.187

Abstract

Using RNA extracted from Zantedeschia aethiopica young leaves and primers designed according to the conservative regions of Araceae lectins, the full-length cDNA of Z. aethiopica agglutinin (ZAA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of zaa was 871 bp and contained a 417 bp open reading frame (ORF) encoding a lectin precursor of 138 amino acids. Through comparative analysis of zaa gene and its deduced amino acid sequence with those of other Araceae species, it was found that zaa encoded a precursor lectin with signal peptide. Secondary and three-dimensional structure analyses showed that ZAA had many common characters of mannose-binding lectin superfamily and ZAA was a mannose-binding lectin with three mannose-binding sites. Southern blot analysis of the genomic DNA revealed that zaa belonged to a multi-copy gene family.

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