Purification of viral neuraminidase from inclusion bodies produced by recombinant Escherichia coli.

Neuraminidase (NA) is one of the targets for the development of new antivirals against the influenza virus. The recombinant Escherichia coli cells, namely the strains BL21(DE3)pLysS and ArcticExpress(DE3) were used to produce the influenza virus neuraminidase. Although the different conditions of induction were tested, the accumulation of over-expressed NA in insoluble fraction occurred independently of these conditions.

Bioaccumulation and biosorption of zinc by a novel Streptomyces K11 strain isolated from highly alkaline aluminium brown mud disposal site.

Zinc biosorption and bioaccumulation by a novel extremely Zn tolerant Streptomyces K11 strain isolated from highly alkaline environment were examined. Temperature, similarly as biosorbent preparation, has negligible effect on the biosorption capacity but very strong effect on the process kinetics. Initial adsorption rate increased almost 10 times with the temperature increase from 10 to 50 °C and it was 30 times higher when non-dried biomass was used.

Characterization of the N-Terminal Catalytic Domain of Lytµ1/6, an Endolysin from Streptomyces aureofaciens Phage µ1/6.

Previous characterization of Lytµ1/6, an endolysin from Streptomyces aureofaciens phage µ1/6, suggested that the N-terminal domain is responsible for the catalytic activity of Lytµ1/6. Mutational analyses (deletions and site-directed mutagenesis) demonstrated that lytic activity of Lytµ1/6 relies on the N-terminal part of about 200 amino acid residues. Various C-terminally truncated versions of Lytµ1/6 failed to cause lysis, indicating the necessity of the CBD for full enzyme activity.

Bacteriophage endolysin Lyt μ1/6: characterization of the C-terminal binding domain.

The gene product of orf50 from actinophage μ1/6 of Streptomyces aureofaciens is a putative endolysin, Lyt μ1/6. It has a two-domain modular structure, consisting of an N-terminal catalytic and a C-terminal cell wall binding domain (CBD). Comparative analysis of Streptomyces phage endolysins revealed that they all have a modular structure and contain functional C-terminal domains with conserved amino acids, probably associated with their binding function.

Analysis of the site-specific integration system of the Streptomyces aureofaciens phage μ1/6.

The bacteriophage μ1/6 integrates its DNA into the chromosome of tetracycline producing strains of Streptomyces aureofaciens by a site-specific recombination process. A bioinformatic analysis of the μ1/6 genome revealed that orf5 encodes a putative integrase, a basic protein of 416 amino acids. The μ1/6 integrase was found to belong to the integrase family of site-specific tyrosine recombinases.