The antibacterial peptide seminal plasmin alters permeability of the inner membrane of E. coli.

Abstract:

: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 with 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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Sitaram N,Krishnakumari V,Nagaraj R

doi

10.1016/0014-5793(92)80535-o

keywords:

subject

Has Abstract

pub_date

1992-06-01 00:00:00

pages

265-8

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80535-O

journal_volume

303

pub_type

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