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CRISPER Gene Therapy Recent Trends and Clinical Applications
Published in Yashwant Pathak, Gene Delivery, 2022
Prachi Pandey, Jayvadan Patel, Samarth Kumar
CRISPR loci were reported to be almost palindromic and were first detected in the iap gene (gene instigating the alkaline phosphatase isozyme conversion) of Escherichia coli inside an intergenic region upstream to the gene. These DNA repeats were also noticed in many bacterial species, like Mycobacterium tuberculosis and Streptococcus pyogenes, as well as in a few archaeal species; namely Haloferax mediterranei, Haloferax volcanii, Thermotoga Maritima, along with filamentous cyanobacterium Anabaena species.
Orders Norzivirales and Timlovirales
Published in Paul Pumpens, Peter Pushko, Philippe Le Mercier, Virus-Like Particles, 2022
Paul Pumpens, Peter Pushko, Philippe Le Mercier
The AP205 platform contributed by the generation of novel protein cages to be employed by the plug-and-display SpyTag/SpyCatcher methodology (Bruun et al. 2018). Thus, the i301 nanocage, which mimicked the structure of VLPs, was based on the 2-keto-3-deoxy-phosphogluconate aldolase from the Entner−Doudoroff pathway of the hyperthermophilic bacterium Thermotoga maritima. The i301 had five mutations that altered the interface between the wild-type protein trimer, promoting assembly into a higher-order dodecahedral 60-mer. The novel modular antigen was designed by fusing SpyCatcher to the N-terminus of the protein and compared with the AP205 VLPs for the ruggedness and immunogenicity of the scaffold, when different transmission-blocking and blood-stage malaria antigens were displayed (Bruun et al. 2018).
VLP Vaccines
Published in Paul Pumpens, Single-Stranded RNA Phages, 2020
The AP205 platform contributed by the generation of novel protein cages to be employed by the plug-and-display SpyTag/SpyCatcher methodology (Bruun et al. 2018). Thus, the i301 nanocage, which mimicked the structure of VLPs, was based on the 2-keto-3-deoxy-phosphogluconate aldolase from the Entner−Doudoroff pathway of the hyperthermophilic bacterium Thermotoga maritima. The i301 had five mutations that altered the interface between the wild-type protein trimer, promoting assembly into a higher-order dodecahedral 60-mer. The novel modular antigen was designed by fusing SpyCatcher to the N-terminus of the protein and compared with the AP205 VLPs for the ruggedness and immunogenicity of the scaffold, when different transmission-blocking and blood-stage malaria antigens were displayed (Bruun et al. 2018).
Characterization of the phosphotransacetylase-acetate kinase pathway for ATP production in Porphyromonas gingivalis
Published in Journal of Oral Microbiology, 2019
Yasuo Yoshida, Mitsunari Sato, Takamasa Nonaka, Yoshiaki Hasegawa, Yuichiro Kezuka
X-ray diffraction data were collected using beamline NE3A at the Photon Factory Advanced Ring (Ibaraki, Japan) at 95 K. Crystals of PgPta and PgAck were cryoprotected by soaking briefly in mother liquor containing 10% (v/v) 2-methyl-2,4-pentanediol and 30% (w/v) PEG 3350, respectively. Diffraction data were indexed, integrated, and scaled using DIALS [36] and SCALA [37] as implemented in XIA2 [38]. The structures of PgPta and PgAck were solved by molecular replacement using MOLREP [39]. Search models were generated using the homology modeling server SWISS-MODEL [40] based on the structure of Pta from Methanosarcina thermophila (MtPta) [Protein Data Bank (PDB) ID: 2AF4] [41] and Ack from Thermotoga maritima (PDB ID: 2IIR) for PgPta and PgAck, respectively. The resultant structures were progressively refined by fitting to the electron density maps using COOT [42]. Manual adjustment of structures was interspersed with refinement cycles using REFMAC5 [43]. Final statistics for X-ray diffraction data and crystallographic refinement are summarized in Table 2.
Biochemical mechanism and biological effects of the inhibition of silent information regulator 1 (SIRT1) by EX-527 (SEN0014196 or selisistat)
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2020
Sylvain Broussy, Hanna Laaroussi, Michel Vidal
The mechanism of SIRT1 inhibition by EX-527 is represented in Figure 2(B), adapted from Gertz et al.25. Mechanistic studies on SIRT1, SIRT3, and Sir2Tm (sirtuin from Thermotoga maritima) demonstrated in all three cases that the inhibition by EX-527 was non-competitive with substrate and uncompetitive with NAD+. Therefore, the inhibition potency depends on the NAD+ concentration. Binding parameters are summarised in Table 2. Kd values for EX-527 measured for the apo enzymes and in the presence of NAD+ confirmed the uncompetitive nature of the inhibition. Indeed, EX-527 does not bind to the apo enzyme, but binds with low micromolar affinity in the presence of NAD+.