scholarly journals Cloning and identification of a novel sperm binding protein, HEL-75, with antibacterial activity and expressed in the human epididymis

2008 ◽  
Vol 23 (9) ◽  
pp. 2086-2094 ◽  
Author(s):  
Y.Q. Lin ◽  
J.Y. Li ◽  
H.Y. Wang ◽  
J. Liu ◽  
C.L. Zhang ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Binding Protein ◽  
Human Epididymis ◽  
Sperm Binding

scholarly journals Antibacterial properties of the sperm-binding proteins and peptides of human epididymis 2 (HE2) family; salt sensitivity, structural dependence and their interaction with outer and cytoplasmic membranes of Escherichia coli

2003 ◽  
Vol 372 (2) ◽  
pp. 473-483 ◽  
Author(s):  
Suresh YENUGU ◽  
Katherine G. HAMIL ◽  
Charles E. BIRSE ◽  
Steven M. RUBEN ◽  
Frank S. FRENCH ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Antibacterial Activity ◽  
Binding Proteins ◽  
Antibacterial Properties ◽  
Antibacterial Activities ◽  
Full Length ◽  
Duration Of Treatment ◽  
Human Epididymis ◽  
Sperm Binding ◽  
Proteins And Peptides

During passage through the epididymis, sperm interact with secreted epididymal proteins that promote maturation, including the acquisition of motility and fertilization competence. Viewed previously as distinct from sperm maturation, host defence capabilities are now recognized functions of the human epididymis 2 (HE2) family of sperm-binding proteins. We analysed the potent dose and time-dependent bactericidal activity of recombinant HE2α, HE2β1 and HE2β2 and found that the full-length proteins (10 μg/ml or ~1 μM) caused more than a 50% decrease in Escherichia coli colony forming units within 15 min. By contrast, human β-defensin-1, at a similar concentration, required more than 90 min to exhibit similar antibacterial activity. The epididymis-specific lipocalin, LCN6, failed to kill bacteria. Higher concentrations (25–100 μg/ml) of HE2 proteins and a longer duration of treatment resulted in near total inhibition of bacterial growth. The C-terminal peptides of HE2α, HEβ1 and HEβ2 proteins exhibited antibacterial activity similar to their full-length counterparts, indicating that the antibacterial activity of HE2 proteins resides in these C-terminal regions. Antibacterial activities of HE2 proteins and peptides were slightly inhibited by NaCl concentrations of up to 150 mM, while human β-defensin-1 activity was nearly eliminated. Reduction and alkylation of disulphide bonds in HE2 proteins and their C-terminal peptides abolished their antibacterial activity. Consistent with the ability to kill bacteria, full-length HE2 proteins and C-terminal peptides caused rapid dose-dependent permeabilization of outer and cytoplasmic E. coli membranes. A much longer exposure time was required for human β-defensin-1-mediated permeabilization of membranes, suggesting a possible difference in mode of action compared with the HE2 antibacterial peptides.

scholarly journals Epididymosomes Transfer Epididymal Sperm Binding Protein 1 (ELSPBP1) to Dead Spermatozoa During Epididymal Transit in Bovine1

2012 ◽  
Vol 87 (4) ◽  
Author(s):  
Olivier D'Amours ◽  
Gilles Frenette ◽  
Louis-Jean Bordeleau ◽  
Nancy Allard ◽  
Pierre Leclerc ◽  
...  
Keyword(s):  
Binding Protein ◽  
Epididymal Sperm ◽  
Sperm Binding

scholarly journals Identification and preliminary characterization of a sperm-binding protein in normal human semen

Reproduction ◽  
1985 ◽  
Vol 73 (1) ◽  
pp. 71-77 ◽  
Author(s):  
P. Abrescia ◽  
G. Lombardi ◽  
M. De Rosa ◽  
L. Quagliozzi ◽  
J. Guardiola ◽  
...  
Keyword(s):  
Binding Protein ◽  
Human Semen ◽  
Preliminary Characterization ◽  
Sperm Binding ◽  
Normal Human

Molecular analysis of cDNA coding for ZP3, a sperm binding protein of the mouse zona pellucida

1988 ◽  
Vol 127 (2) ◽  
pp. 287-295 ◽  
Author(s):  
Maurice J. Ringuette ◽  
Margaret E. Chamberlin ◽  
Anne W. Baur ◽  
Donna A. Sobieski ◽  
Jurrien Dean
Keyword(s):  
Molecular Analysis ◽  
Zona Pellucida ◽  
Binding Protein ◽  
Sperm Binding

An Androgen-Regulated Sperm-Binding Protein

1987 ◽  
Vol 513 (1 Cell Biology) ◽  
pp. 554-556
Author(s):  
N. J. CHAREST ◽  
D. R. JOSEPH ◽  
E. M. WILSON ◽  
F. S. FRENCH
Keyword(s):  
Binding Protein ◽  
Sperm Binding

scholarly journals Identification of the Sea Urchin 350-kDa Sperm-binding Protein as a New Sialic Acid-binding Lectin That Belongs to the Heat Shock Protein 110 Family

2003 ◽  
Vol 278 (43) ◽  
pp. 42050-42057 ◽  
Author(s):  
Eri Maehashi ◽  
Chihiro Sato ◽  
Kaoru Ohta ◽  
Yoichiro Harada ◽  
Tsukasa Matsuda ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Sea Urchin ◽  
Binding Protein ◽  
Sperm Binding ◽  
Sialic Acid Binding ◽  
Binding Lectin
Sign in / Sign up

Export Citation Format

Share Document