Piscicolin 126 is a class IIa bacteriocin isolated from Carnobacterium piscicola JG126 that exhibits strong activity against Listeria monocytogenes. The gene encoding mature piscicolin 126 (m-pisA) was cloned into an Escherichia coli expression system and expressed as a thioredoxin-piscicolin 126 fusion protein that was purified by affinity chromatography. Purified recombinant piscicolin 126 wa...

Proteolytic degradation of recombinant proteins represents a major problem related to production of gene products in heterologous hosts. Recombinant DNA technology offers several alternative strategies for stabilization of expressed gene products. These strategies can often give dramatic stabilization effects and can be combined with strategies involving optimization of fermentation conditions ...

conclusions in conclusion, we developed a method to express the papg.acma protein on the surface of lactobacillus. this is the first report on the successful application of lactic acid bacteria displaying the papg.acma fusion protein. it will be interesting to determine the immune responses against the papg protein in near future using this surface display strategy. results the papg.acma fusion...

The purification of recombinant proteins by affinity chromatography is one of the most efficient strategies due to the high recovery yields and purity achieved. However, this is dependent on the availability of specific affinity adsorbents for each particular target protein. The diversity of proteins to be purified augments the complexity and number of specific affinity adsorbents needed, and t...

Degradation pathways of insoluble proteins have been analyzed in Escherichia coli by using a N-terminal beta-galactosidase fusion protein (VP1LAC) that aggregates immediately after its synthesis. In recombinant E. coli cells, lower molecular mass products, antigenically related to the entire fusion, accumulate together with the entire fusion. In absence of protein synthesis, the insoluble intac...

Vesicles assembled from folded, globular proteins have potential for functions different from traditional lipid or polymeric vesicles. However, they also present challenges in understanding the assembly process and controlling vesicle properties. From detailed investigation of the assembly behavior of recombinant fusion proteins, this work reports a simple strategy to engineer protein vesicles ...

Brucella abortus is a facultative intracellular gram-negative bacterial pathogen that causes abortion in pregnant cattle and undulant fever in humans. The immunogenic B. abortus ribosomal protein L7/L12 is a promising candidate antigen for the development of subunit vaccines against brucellosis. It has already been expressed in several bacteria and has been used as DNA vaccine. In order to cons...

Recombinant protein production has been widely applied for therapeutic and diagnostic applications, namely for polyclonal antibody production. Antibodies are usually raised against a specific protein by immunisation of animals with the purified protein. The Escherichia coli host cell is widely used for the bioproduction of proteins with biomedical interest but some of them are still difficult t...

Recombinant gene strategies using fusion tags for purification are essential procedures to obtain large protein quantities. However, most cloning systems result in recombinant proteins with added amino acids inexistent in their native forms which can lead to significant changes in protein properties. An original and simple cloning strategy is proposed to obtain proteins identical in amino acid ...