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Submitted on December 15, 2003
Accepted on March 8, 2004
Laboratories for Reproductive Biology, Department of Pediatrics, University of North Carolina, Chapel Hill, NC 27599-7500, U.S.A.
* To whom correspondence should be addressed. E-mail: shh{at}med.unc.edu.
Spermatozoa bind a variety of proteins as they pass through the proximal regions of the epididymis where they acquire forward motility and fertilizing ability. Recent evidence indicates that certain epididymis-specific secretory proteins that bind sperm have antibacterial activity and may function as part of the innate immune system. We reported earlier that ESC42, now designated human 
-defensin 118 (DEFB118) is a sperm-binding protein. In this study, we demonstrate that DEFB118 has potent antibacterial activity that is dose, time and structure dependent. Incubation of Escherichia coli for 60 min with 10 µg/ml DEFB118 reduced bacterial survival to 20% and 25 µg/ml reduced survival to 5% of the control. DEFB118 concentrations of 50 and 100 µg/ml, further reduced survival to less than 2% and 1% respectively. A biphasic effect of salt concentration on the antibacterial activity of DEFB118 was observed. Reduction of disulfide bonds and alkylation of cysteines resulted in complete loss of antibacterial activity. DEFB118 caused rapid permeabilization of both outer and inner membranes of Escherichia coli and striking morphological alterations in the bacterial surfaces visible by scanning electron microscopy consistent with a membrane disruptive mechanism of bacterial killing. In contrast, eukaryotic cell membranes were not permeabilized by DEFB118 as indicated by the rat erythrocyte hemolytic assay. Studies on DEFB118 inhibition of macromolecular synthesis and membrane permeability in Escherichia coli were consistent with a primary effect at the cell membrane level. DEFB118 may contribute to epididymal innate immunity and protect the sperm against attack by microorganisms in the male and female reproductive tracts.
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