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Antimicrobial Agents and Chemotherapy, February 2004, p. 673-676, Vol. 48, No. 2
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.2.673-676.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Antimicrobial Activity and Bacterial-Membrane Interaction of Ovine-Derived Cathelicidins

Rachel C. Anderson,1 Robert E. W. Hancock,2 and Pak-Lam Yu1*

Biotechnology Group, Institute of Technology and Engineering, College of Sciences, Massey University, Palmerston North, New Zealand,1 Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia V6T IZ3, Canada2

Received 28 July 2003/ Returned for modification 10 September 2003/ Accepted 15 October 2003

Three ovine-derived cathelicidins, SMAP29, OaBac5mini, and OaBac7.5mini, were compared with respect to their antibacterial activities and interactions with membranes. SMAP29 was confirmed to be {alpha}-helical, broad spectrum, and able to disrupt both the outer and the cytoplasmic membranes at relatively low concentrations. In contrast, the two proline- and arginine-rich OaBac peptides had more-modest antibacterial activities, reduced levels of lipopolysaccharide binding, and a lesser ability to depolarize the cytoplasmic membrane, consistent with a cytoplasmic target.

* Corresponding author. Mailing address: Biotechnology Group, Institute of Technology and Engineering, College of Sciences, Massey University, Private Bag 11-222, Palmerston North, New Zealand. Phone: 64-6-350-5027. Fax: 64-6-350-5604. E-mail: p.yu{at}massey.ac.nz.

Antimicrobial Agents and Chemotherapy, February 2004, p. 673-676, Vol. 48, No. 2
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.2.673-676.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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