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Microbiology 143 (1997), 1533-1537; DOI  10.1099/00221287-143-5-1533
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The outer membrane of lipid A-deficient Escherichia coli mutant LH530 has reduced levels of OmpF and leaks periplasmic enzymes

Marjatta Nurminen, Laura Hirvas and Martti Vaara

Department of Bacteriology and Immunology, Haartman Institute, PO Box 21 (Haartmaninkatu 3), SF-00014 University of Helsinki, Helsinki, Finland

ABSTRACT

We have previously described a new Escherichia coli K-12 mutant, LH530, which has a defective outer membrane. LH530 is very sensitive to hydrophobic antibiotics, does not grow at 42 ° and synthesizes reduced amounts of lipid A. Phenotypically LH530 is very similar to the known lipid A biosynthesis mutants of E. coli and Salmonella typhimurium. Its genetic defect is not known, but the defect is suppressed by multiple copies of ORF195. Here we show that at 37 ° LH530 contains a reduced amount of the OmpF porin and that it leaks periplasmic °-lactamase at 37 °. and 42 °. We further show that ORF195, when present at low copy number, restores the antibiotic resistance and lipid A biosynthesis of LH530 at 28 °, but not at higher temperatures. In contrast, OmpF expression is restored at 37 °.

Author for correspondence: Marjatta Nurminen. Fax: +358 4346382.


Keywords: Escherichia coli, ORF195, OmpF, periplasmic enzymes, outer membrane permeability




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