Fusion of genes encoding Escherichia coli heat-stable enterotoxin and outer membrane protein OmpC
نویسندگان
چکیده
منابع مشابه
Extracellular secretion of Escherichia coli heat-stable enterotoxin I across the outer membrane.
Escherichia coli heat-stable enterotoxin Ip (STIp) is an extracellular toxin consisting of 18 amino acid residues that is synthesized as a precursor of pre (amino acid residues 1 to 19), pro (amino acid residues 20 to 54), and mature (amino acid residues 55 to 72) regions. The precursor synthesized in the cytoplasm is translocated across the inner membrane by the general export pathway consisti...
متن کاملRoles of Lipopolysaccharide and the Outer Membrane Protein OmpC on Bacteriophage T4 Infectivity in Escherichia coli
Although previous studies have demonstrated that lipopolysaccharide (LPS) and the outer membrane protein OmpC are required for bacteriophage T4 infectivity in Escherichia coli, it is unclear whether they played a role in binding or in the downstream viral processes that followed. Such processes may vary from phage DNA injection to viral gene expression, assembly, or release. To investigate this...
متن کاملProperties of synthetically produced Escherichia coli heat-stable enterotoxin.
The properties of a synthetically produced peptide composed of the same primary structure of 18 amino acids described for human Escherichia coli heat-stable enterotoxin were compared with those of purified heat-stable toxin obtained by bacterial growth. The dosage required to evoke fluid secretion in the suckling mouse and rat ligated ileal loop assays was the same for both toxins. The antigeni...
متن کاملProtection in rats immunized with Escherichia coli heat-stable enterotoxin.
Rats immunized with a semipurified preparation of the Escherichia coli heat-stable (ST) enterotoxin conjugated with a protein carrier were protected against challenge with semipurified or purified ST and viable organisms of multiple heterologous serotypes that produce only ST (LT-/ST+), but they were not protected against heal-labile (LT) toxin or viable strains which produce LT either alone (L...
متن کاملEnzyme-linked immunosorbent assay for Escherichia coli heat-stable enterotoxin.
The sensitivity of an enzyme-linked immunosorbent assay (ELISA) to detect pure native Escherichia coli heat-stable toxin (ST) and to identify ST-producing strains among clinical isolates was determined. Two synthetically produced ST preparations were used to raise hyperimmune antisera in rabbits and goats: ST(S), which has the same antigenicity as native ST; and ST(C), which is 15-fold more imm...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1989
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.57.11.3663-3665.1989