African Journal of
Biotechnology

  • Abbreviation: Afr. J. Biotechnol.
  • Language: English
  • ISSN: 1684-5315
  • DOI: 10.5897/AJB
  • Start Year: 2002
  • Published Articles: 12487

Full Length Research Paper

Molecular cloning and expression of a novel gene related to legume lectin from Salvia miltiorrhiza Bunge

Wenping Hua
  • Wenping Hua
  • Department of Life Sciences, Shaanxi Xueqian Normal University, Xi?an, Shaanxi 710061, P.R. China; Key Laboratory of the Ministry of Education for Medicinal Resources and Natural Pharmaceutical Chemistry, National Engineering Laboratory for Resource Development of Endangered Crude Drugs in Northwest of China, College of Life Sciences, Shaanxi Normal University, Xi?an 710062, P.R. China.
  • Google Scholar
Limin Han
  • Limin Han
  • Department of Life Sciences, Shaanxi Xueqian Normal University, Xi?an, Shaanxi 710061, P.R. China; Key Laboratory of the Ministry of Education for Medicinal Resources and Natural Pharmaceutical Chemistry, National Engineering Laboratory for Resource Development of Endangered Crude Drugs in Northwest of China, College of Life Sciences, Shaanxi Normal University, Xi?an 710062, P.R. China.
  • Google Scholar
Zhezhi Wang*
  • Zhezhi Wang*
  • Key Laboratory of the Ministry of Education for Medicinal Resources and Natural Pharmaceutical Chemistry, National Engineering Laboratory for Resource Development of Endangered Crude Drugs in Northwest of China, College of Life Sciences, Shaanxi Normal University, Xi?an 710062, P.R. China.
  • Google Scholar


  •  Received: 19 December 2013
  •  Accepted: 13 July 2015
  •  Published: 15 July 2015

Abstract

Lectins have been well studied and proved to play important roles in plant defense but information of legume lectins from non-legume plants has been rarely reported. A new legume lectin gene, designated as SmL1, was cloned from Salvia miltiorrhiza Bunge, a famous traditional Chinese medicinal plant. The cDNA of SmL1 was 919 bp in length and contained an 822 bp open reading frame (ORF) encoding a putative lectin precursor with two legume lectin domains. The deduced SML1 protein of SmL1 shared 29 to 43% identities with other legume lectin sequences. Real time PCR analysis revealed that SmL1 was predominantly expressed in the leaves and could be induced by pathogens and MeJA. The recombinant protein (rSmL1) of SmL1 in Escherichia coli M15 was purified and showed agglutination activity towards rabbit and mouse red blood cells, and anti-bacterial activity against E. coli (ATCC35218), Pseudomonas lachrymans (PSL) and Xanthomonas campestris pv. Campestris (Pammel) Dowson (XC-1). Based on these results, SmL1 could play a role in medicinal plant disease control.

 

Key words: Anti-bacterial activity, gene expression, legume lectin, recombinant protein, Salvia miltiorrhiza Bunge.