Cloning and expression of two plant proteins: similar antimicrobial activity of native and recombinant form.
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.
Capparelli
R
R
School of Biotechnological Sciences, University of Naples Federico II, Via Università 133, Portici, Naples 80055, Italy. capparel@unina.it
Palumbo
D
D
Iannaccone
M
M
Ventimiglia
I
I
Di Salle
E
E
Capuano
F
F
Salvatore
P
P
Amoroso
M G
MG
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology*; D002470:Cell Survival / Q000187:drug effects; D003001:Cloning, Molecular / Q000379:methods*; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology*; D015202:Protein Engineering / Q000379:methods; D011994:Recombinant Proteins / Q000378:metabolism / Q000494:pharmacology; D013210:Staphylococcus / Q000166:cytology / Q000187:drug effects*
D000900:Anti-Bacterial Agents; D010940:Plant Proteins; D011994:Recombinant Proteins; C082942:puroindoline protein, Triticum aestivum