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Infection and Immunity, August 1999, p. 4106-4111, Vol. 67, No. 8
Department of
Medicine1 and Molecular Biology
Institute,4 UCLA School of Medicine, Los
Angeles, California 90095; Department of General Pathology and
Pathophysiology, Institute for Experimental Medicine, 19736 St.
Petersburg, Russia2; and Respiratory and
Neurologic Diseases Research Unit, Midwest Area National Animal
Disease Center, Agricultural Research Service, U.S. Department of
Agriculture, Ames, Iowa 500103
Received 18 March 1999/Returned for modification 11 May
1999/Accepted 19 May 1999
We purified three proline-rich antimicrobial peptides from
elastase-treated extracts of sheep and goat leukocytes and subjected two of them, OaBac5
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Purification and Properties of Proline-Rich
Antimicrobial Peptides from Sheep and Goat Leukocytes
and ChBac5, to detailed analysis. OaBac5
and
ChBac5 were homologous to each other and to bovine Bac5. Both exhibited
potent, broad-spectrum antimicrobial activity under low-concentration
salt conditions. While the peptides remained active against
Escherichia coli, Pseudomonas aeruginosa,
Bacillus subtilis, and Listeria monocytogenes
in 100 mM NaCl, they lost activity against Staphylococcus
aureus and Candida albicans under these conditions.
ChBac5 was shown to bind lipopolysaccharide, a property that could
enhance its ability to kill gram-negative bacteria. Proline-rich Bac5
peptides are highly conserved in ruminants and may contribute
significantly to their innate host defense mechanisms.
*
Corresponding author. Mailing address: Department of
Medicine, UCLA Center for the Health Sciences, 10833 LeConte Ave., Los Angeles, CA 90095-1690. Phone: (310) 825-5340. Fax: (310) 206-8766. E-mail: rlehrer{at}med1.medsch.ucla.edu.
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