Expression and characterization of bovine lactoperoxidase by recombinant vaccinia virus.

Abstract

Lactoperoxidase (LPO) is a 78 kDa heme-containing oxidation-reduction enzyme present in milk, found in physiological fluids of mammals. LPO has an antimicrobial activity, and presumably contribute to the protective functions of milk against infectious diseases. In this study, recombinant vaccinia virus expressing bovine LPO (vv/bLPO) was constructed. In rabbit kidney (RK13) cells infected with vv/bLPO, recombinant bLPO was detected in both cell extracts and culture supernatants. Tunicamycin treatment decreased the molecular weight of recombinant bLPO, indicating that recombinant bLPO contains a N-linked glycosylation site. The replication of recombinant vaccinia viruses expressing bovine lactoferrin (vv/bLF) at a multiplicity of infection (moi) of 5 plaque-forming units (PFU)/cell was inhibited by antiviral activity of recombinant bLF, suggesting that vv/bLF has an antiviral effect against vaccinia virus. On the other hand, the replication of vv/bLPO at a moi of 5 PFU/cell was not inhibited by antiviral activity of recombinant bLPO, indicating that this recombinant virus could be used as a suitable viral vector. These results indicate that a combination of bLPO and vaccinia virus vector may be useful for medical and veterinary applications in vivo.

• Authors: Tetsuya Tanaka, Xuenan Xuan, Asato Kojima, Ikuo Igarashi, Kozo Fujisaki, Kei-Ichi Shimazaki
• Journal: Cytotechnology (Cytotechnology) Vol. 58 Issue 3 Pg. 127-33 (Nov 2008) ISSN: 0920-9069 [Print] United States
• PMID: 19214766 (Publication Type: Journal Article)