scholarly journals Bacterial production of site specific 13C labeled phenylalanine and methodology for high level incorporation into bacterially expressed recombinant proteins

2016 ◽  
Vol 67 (1) ◽  
pp. 23-34 ◽  
Author(s):  
Bhargavi Ramaraju ◽  
Hana McFeeters ◽  
Bernhard Vogler ◽  
Robert L. McFeeters
2011 ◽  
Vol 9 (4) ◽  
pp. 419-433 ◽  
Author(s):  
Andrew J. Conley ◽  
Jussi J. Joensuu ◽  
Alex Richman ◽  
Rima Menassa

2020 ◽  
Vol 8 (2) ◽  
pp. 197
Author(s):  
Shomeek Chowdhury ◽  
Stephen S. Fong

The impact of microorganisms on human health has long been acknowledged and studied, but recent advances in research methodologies have enabled a new systems-level perspective on the collections of microorganisms associated with humans, the human microbiome. Large-scale collaborative efforts such as the NIH Human Microbiome Project have sought to kick-start research on the human microbiome by providing foundational information on microbial composition based upon specific sites across the human body. Here, we focus on the four main anatomical sites of the human microbiome: gut, oral, skin, and vaginal, and provide information on site-specific background, experimental data, and computational modeling. Each of the site-specific microbiomes has unique organisms and phenomena associated with them; there are also high-level commonalities. By providing an overview of different human microbiome sites, we hope to provide a perspective where detailed, site-specific research is needed to understand causal phenomena that impact human health, but there is equally a need for more generalized methodology improvements that would benefit all human microbiome research.


2019 ◽  
Vol 40 (16-17) ◽  
pp. 2125-2128
Author(s):  
Yan Wang ◽  
Mingming Dong ◽  
Mingliang Ye

2002 ◽  
Vol 48 (1) ◽  
pp. 43-48 ◽  
Author(s):  
Donald Tremblay ◽  
Johanne Lemay ◽  
Michel Gilbert ◽  
Yvan Chapdelaine ◽  
Claude Dupont ◽  
...  

Two major antigens from Mycobacterium tuberculosis were produced by Streptomyces lividans as secreted extracellular proteins. An expression-secretion vector had been constructed that contained the promoter of xylanase A and the signal sequence of cellulase A. The latter contained two initiation codons preceded by a Shine-Dalgarno sequence plus eight nucleotides complementary to the 16S rRNA. The genes encoding the 38-kDa (Rv0934) and 19-kDa (Rv3763) proteins, respectively, were amplified by polymerase chain reaction and cloned into that vector. The recombinant proteins were then purified from the culture supernatants of the clones. The yields after purification were 80 mg/L for the 38-kDa protein and 200 mg/L for the 19-kDa protein. Sequence analysis of the N-terminal sequences showed a deletion of seven or eight amino acids for the 38-kDa protein, while in the 19-kDa protein 22 or 23 amino acids were lost, as compared with the respective wild-type proteins. However, the 19 kDa recombinant protein had the same N-terminal sequence as the one recovered from the M. tuberculosis culture supernatant. The high yields obtained for these two proteins demonstrated the potential of S. lividans as an alternative host for the production of recombinant proteins from M. tuberculosis. The culture conditions have yet to be worked out to minimize proteolytic degradation and to recover intact products.Key words: streptomycetes, downstream box, signal peptide, protein secretion, Mycobacterium tuberculosis.


2011 ◽  
Vol 58-59 ◽  
pp. 25-32 ◽  
Author(s):  
Hai Chen ◽  
Yingfei Lu ◽  
Zhengzhi Fang ◽  
Jingxian Liu ◽  
Hong Tian ◽  
...  

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