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ARTICLE

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

ZHONGHAI CHEN¹, YONGZHEN PANG¹, XIAOJUN LIU¹, XINGLONG WANG¹, ZHONGXIANG DENG¹, XIAOFEN SUN¹, KEXUAN TANG^1,2

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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