Abstract：
:The mechanisms of interaction of the recombinant N-terminal portion of bactericidal/permeability-increasing protein, rBPI21, with various planar asymmetric and symmetric bilayer membranes, including the lipid matrix of the outer membrane of Gram-negative bacteria, were investigated via electrical measurements. For the lipopolysaccharide (LPS) leaflet of the outer membrane, isolated deep rough mutant LPS of Escherichia coli strain F515 (F515 LPS) and Proteus mirabilis strain R45 (R45 LPS) were used. The addition of rBPI21 to the LPS side of asymmetric LPS/phospholipid membranes, as well as to black lipid membranes made from dioleoylphosphatidylglycerol (DOPG), led to membrane rupture. The innermembrane potential difference resulted in a slight increase from 0 to 5 mV for symmetric DOPG membranes but changed for asymmetric F515 LPS/PL membranes from -36 to +8 mV and for R45 LPS/PL membranes from -37 to -5 mV following the addition of rBPI21. In all cases, the addition of rBPI21 led to an increase in membrane current. The effect of rBPI21 on the innermembrane potential difference of LPS/PL membranes was significantly reduced in the presence of 40 mM MgCl2 (shift from -36 to -31 mV for F515 LPS). On the basis of these results and from our studies on the interaction of rBPI21 with lipid monolayers and aggregates [Wiese, A., et al. (1997) Biochemistry 36, 10301-10310], a model is discussed explaining how the observed membrane rupture, increase of membrane current, and change of transmembrane potential as induced by rBPI21 may contribute to bacterial dysfunction.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Wiese A,Brandenburg K,Carroll SF,Rietschel ET,Seydel Udoi
10.1021/bi970177esubject
Has Abstractpub_date
1997-08-19 00:00:00pages
10311-9issue
33eissn
0006-2960issn
1520-4995pii
bi970177ejournal_volume
36pub_type
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