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Vizler, C.

Publications and source records attributed to Vizler, C..

2 recordsLinked to original sources

Novel Synthetic Polymyxin Variants Inspired by Newly Uncovered Natural Sequences Explored as Potential Antibiotics

The incidence of infections caused by multidrug-resistant bacterial agents has increased at an alarming rate worldwide. With the aim of identifying novel antimicrobial peptides (AMPs), we screened bacteria isolated from various environmental samples. Our hypothesis was that the sequence space of natural AMPs belonging to known AMP classes is far from saturation. We used a classical pipeline of bacterial culturing, overlay assays, extraction and fractionation to purify AMPs for identification. Using LC/MS analysis, the structure of AMPs isolated from a strain of Paenibacillus was narrowed down and a new subclass of polymyxins was uncovered. These harbor three aliphatic residues within the cyclic C-terminal, and in certain cases Ser replaces Thr at position A2. Four discrete polymyxins fitting the new class, but not identical to the natural polymyxins were synthesized and tested against 29 human pathogenic bacteria. Each displayed an antibacterial spectrum different from that of colistin, with the best candidate surpassing it in potency against ten bacterial strains, but underperforming against three others. These results demonstrate that current screening of natural bacterial isolates can still permit the design of novel antimicrobial peptide variants without the substantial threat of diminishing returns.

microbiology↗

Complex regulation of RETINOBLASTOMA-RELATED's interactions with E2Fs via phosphorylation

Arabidopsis RETINOBLASTOMA-RELATED (RBR) regulates cell proliferation by interacting with E2F transcription factors and DIMERIZATION PARTNER, RB-LIKE, E2F AND MULTI-VULVAL CLASS B COMPLEX (DREAM) components. Although CDK-CYCD phosphorylation is believed to affect RBRs E2F-binding capacity, the precise phosphorylation events inhibiting RBRs cell cycle function remain unclear. This study found RBR phosphorylated at 13 of 16 CDK sites in Arabidopsis, with many phosphorylated forms still binding E2Fs. In contrast, multi-phosphorylated RBR forms with phosphorylated 911S site in Arabidopsis thaliana and corresponding sites in Medicago truncatula or Brassica napus do not co-purify with E2Fs and DREAM components but interact with RNA-binding proteins involved in post-transcriptional regulation through ribosomal biogenesis and protein translation. The 911S phosphorylation is high in proliferating cells and rapidly diminishes under DNA damage conditions, indicating its role in switching from proliferation to quiescence under stress. However, molecular modelling implies that this site is not accessible for phosphorylation if RBR is in complex with E2Fs. These findings suggest that different phosphorylation events inhibit RBRs capacity to form complexes with E2Fs and to release E2Fs from RBR inhibition. We posit that multi-site phosphorylation coupled to 911S impedes free RBRs binding to E2Fs and DREAM components, but this is not the initial inhibitory phosphorylation contributing to the disruption of RBR-E2F-DP complexes. Rather, it facilitates RBR interaction with proteins involved in post-transcriptional cell cycle regulation.

plant biology↗