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Infection and Immunity, November 1999, p. 6139-6144, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Isolation, Characterization, cDNA Cloning, and Antimicrobial Properties of Two Distinct Subfamilies of alpha -Defensins from Rhesus Macaque Leukocytes

Yi-Quan Tang,1 Jun Yuan,1 Christopher J. Miller,2 and Michael E. Selsted1,*

Department of Pathology, University of California, Irvine, California 92697,1 and California Regional Primate Research Center, Center for Comparative Medicine, and School of Veterinary Medicine, University of California, Davis, California 956162

Received 23 June 1999/Returned for modification 6 August 1999/Accepted 20 August 1999

Experiments to isolate and characterize rhesus macaque myeloid alpha -defensins (RMADs) were conducted. Seven RMAD peptides were isolated and sequenced, and the cDNAs encoding six of these peptides and one other alpha -defensin from bone marrow were also characterized. Four of the RMADs were found to be highly similar to human neutrophil alpha -defensins HNP-1 to HNP-3, while the remaining four peptides were much more similar to human enteric alpha -defensin HD-5. Two alpha -defensin pairs differed only by the presence or absence of an additional arginine at the amino termini of their mature peptides, indicative of alternate posttranslational processing. The primary translation products of RMAD-1 to -8 are 94- and 96-amino-acid prepropeptides that are highly similar to those of human alpha -defensins. Immunolocalization experiments revealed a granular cytoplasmic pattern in the cytoplasms of neutrophils, indistinguishable from the pattern observed after immunostaining of human myeloid alpha -defensins in polymorphonuclear leukocytes. Each of the purified peptides was tested for its in vitro activities against Staphylococcus aureus 502a, Listeria monocytogenes EGD, Escherichia coli ML35, and Cryptococcus neoformans 271A. Several of the peptides were microbicidal for the gram-positive bacteria and C. neoformans at defensin concentrations in the range of 2 to 5 µM. All of the peptides were bacteriostatic against E. coli, but none were bactericidal for this organism. This study is the first to characterize the sequences and activities of alpha -defensins from nonhuman primates, data that should aid in delineating the role of these peptides in rhesus macaque host defense.

* Corresponding author. Mailing address: Department of Pathology, College of Medicine, University of California, Irvine, CA 92697-4800. Phone: (949) 824-2350. Fax: (949) 824-2346. E-mail: meselste{at}uci.edu.

Infection and Immunity, November 1999, p. 6139-6144, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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