Biotechnology Letters

, Volume 28, Issue 13, pp 943–949

Cloning and expression of two plant proteins: similar antimicrobial activity of native and recombinant form

  • R. Capparelli
  • D. Palumbo
  • M. Iannaccone
  • I. Ventimiglia
  • E. Di Salle
  • F. Capuano
  • P. Salvatore
  • M. G. Amoroso
Original paper

DOI: 10.1007/s10529-006-9031-9

Cite this article as:
Capparelli, R., Palumbo, D., Iannaccone, M. et al. Biotechnol Lett (2006) 28: 943. doi:10.1007/s10529-006-9031-9

Abstract

Antimicrobial peptides and proteins are being studied with increasing interest because of their broad range antimicrobial activity. Among plant antimicrobial proteins, the wheat seed polypeptides, puroindoline a and puroindoline b, are particularly interesting because of their established antibacterial activity. In this paper we describe different strategies used to clone His tagged and GST tagged puroindolines obtaining 1.5 mg recombinant protein from 1 l culture. The antimicrobial activity of recombinant and native puroindolines was comparable.

Keywords

Antimicrobial activityInnate immunityRecombinant puroindolinesRefoldingMembrane damage

Copyright information

© Springer Science+Business Media B.V. 2006

Authors and Affiliations

  • R. Capparelli
    • 1
  • D. Palumbo
    • 1
  • M. Iannaccone
    • 1
  • I. Ventimiglia
    • 1
  • E. Di Salle
    • 2
  • F. Capuano
    • 3
  • P. Salvatore
    • 4
  • M. G. Amoroso
    • 1
  1. 1.School of Biotechnological SciencesUniversity of Naples “Federico II”Portici, NaplesItaly
  2. 2.Dipartimento di Biochimica e Biotecnologie medicheUniversity of Naples “Federico II”NaplesItaly
  3. 3.Istituto Zooprofilattico Sperimentale per il MezzogiornoPortici, NaplesItaly
  4. 4.Department of Cellular and Molecular Pathology “L. Califano”, School of Biotechnological SciencesUniversity of Naples “Federico II”NaplesItaly