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The antibacterial peptide seminal plasmin alters permeability of the inner membrane of E. coli
Author(s) -
N. Sitaram,
Viswanatha Krishnakumari,
Ramakrishnan Nagaraj
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80535-o
Subject(s) - antibacterial activity , inner membrane , biochemistry , membrane , phosphatidylcholine , peptide , chemistry , membrane permeability , escherichia coli , divalent , bacteria , biology , biophysics , phospholipid , gene , genetics , organic chemistry
Seminal plasmin (SPLN) a 47‐residue peptide, isolated from bovine seminal plasma, exhibits antibacterial activity against Gram‐positive and Gram‐negative bacteria. Although SPLN strongly inhibits the transcription of various natural and synthetic templates by E. coli RNA polymerase in vitro, it also associates mith model membranes of phosphatidylcholine and phosphatidic acid. We have undertaken experiments to ascertain whether SPLN permeabilizes the bacterial inner membrane and thereby exerts its antibacterial activity, as in the case of recently isolated antibacterial peptides from mammalian sources. Our results show that SPLN affects the permeability properties of the bacterial inner membrane which is reflected by increased uptake of ortho ‐nitrophenylgalactoside (ONPG), which can normally be translocated only by protein transporters. SPLN has also been shown to act on the outer membrane, since divalent cations inhibit antibacterial activity.