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Bacteriolytic activity of seminalplasmin
S N Chitnis1, K S Prasad, P M Bhargava
1Centre for Cellular and Molecular Biology, Hyderabad, India.
Journal of General Microbiology
|May 1, 1987
Summary
Seminalplasmin, a protein from bovine seminal fluid, effectively lyses bacteria, with activity influenced by bacterial growth phase and medium. Its lytic action appears to involve activating an autolysin.
Area of Science:
- Microbiology
- Biochemistry
- Protein Chemistry
Background:
- Bovine seminal plasma contains antimicrobial proteins.
- Seminalplasmin exhibits broad-spectrum antibacterial activity.
Purpose of the Study:
- To characterize the lytic activity of seminalplasmin.
- To investigate the mechanism of seminalplasmin-mediated bacterial lysis.
Main Methods:
- Assessing seminalplasmin's lytic effect on Gram-positive and Gram-negative bacteria and Candida albicans.
- Investigating the influence of temperature, heat treatment, growth phase, and growth medium on bacterial susceptibility.
- Examining the effect of inhibitors and divalent cations on lytic activity.
Main Results:
- Seminalplasmin lysed bacteria but not fungi.
- Lytic activity was independent of lysozyme and RNA/protein synthesis inhibitors.
- Activity was inhibited by divalent cations (Ca2+, Mn2+, Mg2+) and dependent on bacterial growth phase and medium composition.
- Optimal lysis occurred at 37°C, with heat-treated bacteria showing reduced susceptibility.
Conclusions:
- Seminalplasmin possesses unique antibacterial properties distinct from lysozyme.
- Bacterial cell physiology significantly impacts susceptibility to seminalplasmin.
- The lytic mechanism likely involves the activation of bacterial autolysins.