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Article
Open AccessModulating endotoxin activity by combinatorial bioengineering of meningococcal lipopolysaccharide
Neisseria meningitidis contains a very potent hexa-acylated LPS that is too toxic for therapeutic applications. We used systematic molecular bioengineering of meningococcal LPS through deletion of biosynthetic en...
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Article
Phase variation of Opa proteins of Neisseria meningitidis and the effects of bacterial transformation
Opa proteins are major proteins involved in meningococcal colonization of the nasopharynx and immune interactions. Opa proteins undergo phase variation (PV) due to the presence of the 5′-CTCTT-3′ coding repeat...
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Protocol
Construction of porA Mutants
The PorA or class 1 protein is one of the major meningococcal outermembrane proteins (OMPs). It is one of the two porins found in this organism, the other one being the PorB or class 2/3 protein. It folds into...
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Protocol
Construction of LPS Mutants
Lipopolysaccharide (LPS) is a major component of the meningococcal outer membrane. It consists of a hexa-acylated glucosamine disaccharide substituted at both ends with diphosphoethanolamine, to which an oligo...
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Article
Meningitis bacterium is viable without endotoxin
The outer membrane of Gram-negative bacteria contains lipopolysaccharide (LPS) as its outer monolayer. This is anchored to the membrane by lipid A, which is responsible for LPS's activity as an endotoxin1. In Esc...
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Article
Response of Neisseria meningitidis to iron limitation
In the human body, the concentration of free iron is limiting for bacterial growth, since iron is bound to transport and storage proteins such as transferrin and lactoferrin. When grown under iron starvation, ...
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Article
Analysis of structure-function relationships in Escherichia coli K12 outer membrane porins with the aid of ompC-phoE and phoE-ompC hybrid genes
To study structure-function relationships in the outer membrane pore proteins OmpC and PhoE of Escherichia coli K12, we have constructed a series of phoE-ompC hybrid genes in which DNA encoding part of one protei...
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Article
Cloning of ompF, the structural gene for an outer membrane pore protein of E. coli K12: Physical localization and homology with the phoE gene
The ompF gene of Escherichia coli K12, which is the structural gene for an outer membrane pore protein has been cloned into the multicopy plasmid vector pACYC184. Expression of the cloned ompF gene results in ove...
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Article
Genetic and biochemical characterization of anEscherichia coli K-12 mutant with an altered outer membrane protein
The properties of anEscherichia coli K-12 mutant are described which seemingly produces a “new” major outer membrane protein with an apparent molecular weight of 40000. This 40K protein was purified and its cyano...
