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Bennett, B. C.

Publications and source records attributed to Bennett, B. C..

2 recordsLinked to original sources

Gain and Loss of Acquired Doxycycline Resistance in Lactiplantibacillus plantarum: An Adaptive Laboratory Evolution Study

Probiotics interact in a mutualistic way with humans. Exposure of probiotics to sublethal concentrations of commonly prescribed antibiotics can cause resistance to arise. Over 1000 generations, we performed an adaptive laboratory evolution (ALE) experiment to determine if the fitness of the probiotic Lactobacillus plantarum is altered by exposure to doxycycline (DOX) at 1/10 MIC. Compared to the original culture, L. plantarum exposed to sublethal DOX acquired modest resistance ([~]4-fold) over time. When the selection pressure was removed, resistance was lost rapidly, in [~]50 generations. This suggests that resistance, once acquired, is not fixed. The mechanism by which resistance is acquired and subsequently lost was investigated by whole genome sequencing (WGS). Analysis of the single nucleotide variants (SNVs) identified in the WGS of the generation 1000 DOX-treated cultures reveal 16 distinct variants across 15 genes. Two of these variants are in the rpsJ gene, which encodes ribosomal protein s10, a component of the 30S ribosomal subunit, and result in non-synonymous mutations (H56Y and S94N). This gene has been previously reported to harbor mutations associated with tetracycline class resistance, including DOX and tigecycline. WGS of archived cells from generations 350 and 750 reveals that one of these rpsJ variants (H56Y) arises early in the experiment. Additional rpsJ variants at position 57 (K57M, K57I) could be identified within intermediate generations. Most rpsJ SNVs identified from the WGS could be verified by colony PCR and Sanger sequencing. Importantly, no rpsJ variants are observed in the original culture sequences or in same-generation controls. ImportanceProbiotics are beneficial bacteria often found in fermented foods and beverages. When consumed, they can colonize the gut and provide several advantages. Antibiotics, even at levels too low to kill bacteria, can exert pressure that leads to antibiotic resistance. Though well-studied in harmful bacteria, it is less understood what effects this may have on probiotics. Using experimental evolution, we grew a popular probiotic, Lactiplantibacillus plantarum, in the presence of a low concentration of doxycycline, one of the most highly prescribed antibiotics in the US. Over the course of 5 months, roughly a thousand generations, the probiotic became [~]4-fold more resistant; once we removed the antibiotic and continued the experiment, this resistance disappeared rapidly. DNA sequencing identified variants in the rpsJ gene, which encodes a protein important for translation. As doxycycline interferes with this process, the rpsJ variants may underlie the emergence of modest resistance we observe.

microbiology↗

A Constitutively Closed Pannexin1 Channel in Lipid Bilayer Nanodiscs Assembles as a Large-Pore Heptamer

Pannexin 1 (Panx1) channels are widely expressed and play important roles in apoptotic cell clearance, inflammation, blood pressure regulation, neurological disorders, opiate withdrawal, and cancer progression and metastasis. We performed (1) physicochemical analysis on a constitutively closed Panx1 channel (designated fPanx1{Delta}C) to examine the entire population of particles to detect multiple oligomeric states and (2) cryoEM in the membrane mimetics amphipol A8-35 and lipid bilayer nanodiscs. Our results reveal that the dominant if not exclusive oligomeric state of fPanx1{Delta}C is a heptamer, in solution and by cryoEM. The Panx1 heptamer provides further structural diversity within the family of large-pore channels, including hexameric LRRC8 (SWELL1) channels and connexin hemichannels, octameric CALHM1 channels and innexin hemichannels, and undecameric CALHM2 channels. Conserved structural themes are a large cytoplasmic vestibule with a diameter that corresponds roughly with the oligomeric state and a 4-helix bundle protomer, albeit with noncanonical helical packing for CALHM1 and CALHM2. In BriefThe 4-helix bundle protomer of a constitutively closed pannexin1 channel assembles as a heptamer in solution and by cryoEM.

biophysics↗