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Escherichia coli

About: Escherichia coli is a research topic. Over the lifetime, 59041 publications have been published within this topic receiving 2050337 citations. The topic is also known as: E. coli & E coli jdj.


Papers
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Journal ArticleDOI
15 Jul 1988-Gene
TL;DR: Vectors were constructed that allow foreign peptides to be expressed in Escherichia coli as fusion proteins that can be directed to the periplasm by including the leader sequence from the phoA gene on the vector.

640 citations

Book ChapterDOI
TL;DR: This chapter discusses the major techniques and parameters that affect transformation of bacteria, focusing on E.coli, and the genetic constitution of the host strain of the organism being transformed.
Abstract: Publisher Summary Escherichia coli is a universal host organism both for molecular cloning of DNA and for a diverse set of assays involving clones genes. This chapter discusses the major techniques and parameters that affect transformation of bacteria, focusing on E.coli . There are two major parameters involved in efficiently transforming a bacterial organism. The first is the method used to induce competence for transformation. There are two primary technical variations in this method: chemical induction of competence and high-voltage electroshock treatment (electroporation). Both the characteristic of the cells being transformed and the purpose of the transformation affect the choice of method. The second major parameter is the genetic constitution of the host strain of the organism being transformed; a variety of genes can dramatically influence the outcome of transformation experiments.

633 citations

Journal ArticleDOI
TL;DR: A new adhesive factor was found to occur with greater frequency in EPEC strains and was distinct from type 1 pili and was not inhibited by the presence ofD-mannose.
Abstract: Escherichia coli strains isolated from outbreaks of diarrheal disease were tested for the presence of adhesive factors. Fifty-one of these strains belonged to traditional infantile entero-pathogenic serotypes (EPEC) and 17 belonged to other serotypes. None of these strains were enterotoxigenic and none possessed colonization factors CFA/I or CFA/II, which have been described among strains of enterotoxigenicE. coli (ETEC). EnterotoxigenicE. coli strains from patients with diarrhea and strains which were neither EPEC nor ETEC from subjects without diarrhea were also examined. By means of a tissue culture technique using HEp-2 cells, a new adhesive factor was found to occur with greater frequency in EPEC strains. The adhesive factor was found less frequently in the other groups ofE. coli studied. It was distinct from type 1 pili and was not inhibited by the presence ofD-mannose.

631 citations

Journal ArticleDOI
Jong Hyun Choi1, Sang Yup Lee1
TL;DR: Recent advances in secretory and extracellular production of recombinant proteins using E. coli are discussed, including the twin-arginine translocation system, which has recently been employed for the efficient secretion of folded proteins.
Abstract: Escherichia coli is one of the most widely used hosts for the production of recombinant proteins. However, there are often problems in recovering substantial yields of correctly folded proteins. One approach to solve these problems is to have recombinant proteins secreted into the periplasmic space or culture medium. The secretory production of recombinant proteins has several advantages, such as simplicity of purification, avoidance of protease attack and N-terminal Met extension, and a better chance of correct protein folding. In addition to the well-established Sec system, the twin-arginine translocation (TAT) system has recently been employed for the efficient secretion of folded proteins. Various strategies for the extracellular production of recombinant proteins have also been developed. For the secretory production of complex proteins, periplasmic chaperones and protease can be manipulated to improve the yields of secreted proteins. This review discusses recent advances in secretory and extracellular production of recombinant proteins using E. coli.

628 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
20242
20232,609
20225,796
20211,236
20201,337
20191,412