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Adams, L. A.

Publications and source records attributed to Adams, L. A..

3 recordsLinked to original sources

Microbial functional guilds and genes are key to explaining soil nutrient cycling alongside soil and plant variables

Microbes play central roles in soil nutrient cycling, yet a limited range of microbial community characteristics have been used to explain ecosystem nutrient cycling rates and their importance relative to plant and abiotic factors remains unclear. In this study, we assessed which of 126 commonly measured soil fungal and bacterial community characteristics best explained soil nitrogen (N) and phosphorus (P) cycling rates in temperate forests in the Northeastern U.S., as well as the relative contributions of microbial, plant, and abiotic factors. Using boosted regression tree modeling, we identified the microbial variables with the highest contributions to models explaining nutrient cycling rates: the relative abundances of ectomycorrhizal fungi and N-decomposition genes from oligotrophic bacteria were the most important for net ammonification, the relative abundances of indicator taxa in bacterial networks, nitrifying bacteria, and copiotrophic bacteria were the most important for net nitrification, and the relative abundance of fungal P-cycling oxidoreductase genes was the most important for net soil phosphate change. Microbial variables explained more variation than plant and abiotic variables in multivariate linear models of net nitrification and net phosphate release rates, but not net ammonification rates, which were largely explained by soil edaphic factors. Leaf litter traits were also important in explaining variation in net nitrification rates, and soil temperature was important in explaining rates of net phosphate release in soil. Collectively, our findings suggest that the N-cycling capacity of microbial functional guilds and fungal community P-cycling capacity should be incorporated into ecosystem biogeochemical models to improve our predictions and understanding of nutrient cycling and related ecological processes.

ecology↗

Green synthesized silver nanoparticles from Moringa: Potential for preventative treatment of SARS-CoV-2 contaminated water

Biogenic silver nanoparticles have been reported as good antimicrobial candidates. Thus, this study investigated the antiviral activity of silver nanoparticles synthesized against SARS-CoV-2. The silver nanoparticle was biosynthesized using leave extracts of Moringa oleifera (AgNPmo) and characterized using UV-Vis spectroscopy, Fourier transform infrared spectroscopy (FTIR), scanning electron microscopy, and X-ray diffractometry (XRD). The AgNPmo was first tested on clinical bacterial isolates, Pseudomonas aeruginosa (ATTC 154423) and Staphylococcus aureus (ATTC 209233), to ascertain its antimicrobial potential. In-vitro studies were also conducted to determine the cytotoxicity effect of AgNPmo on Vero cells. The efficacy and concentration of AgNPmo against SARS-CoV-2 were evaluated using a qPCR assay in a dose-dependent manner. The results demonstrated the successful biosynthesis and characterization of AgNPmo and its efficacy against the bacterial isolates. The AgNPmo showed low toxicity on the Vero cells. The IC50 from the cytotoxicity assay demonstrated the antiviral activity of the AgNPmo on the SARS-CoV-2 virus, leading to an increase in the Cycle threshold values, notably at 48 hours of incubation and at low concentrations. The results showed that the biogenic AgNPmo synthesized was cost-effective and showed both antimicrobial and antiviral potentials. These findings suggest that the nanoparticles could be a promising alternative for combating SARS-CoV-2, especially for water purification and preventing transmission.

microbiology↗

Altered conformational sampling along an evolutionary trajectory changes the catalytic activity of an enzyme

Several enzymes are known to have evolved from non-catalytic proteins such as solute-binding proteins (SBPs). Although attention has been focused on how a binding site can evolve to become catalytic, an equally important question is: how do the structural dynamics of a binding protein change as it becomes an efficient enzyme? Here we performed a variety of experiments, including double electron-electron resonance (DEER), on reconstructed evolutionary intermediates to determine how the conformational sampling of a protein changes along an evolutionary trajectory linking an arginine SBP to a cyclohexadienyl dehydratase (CDT). We observed that primitive dehydratases predominantly populate catalytically unproductive conformations that are vestiges of their ancestral SBP function. Non-productive conformational states are frozen out of the conformational landscape via remote mutations, eventually leading to extant CDT that exclusively samples catalytically relevant compact states. These results show that remote mutations can reshape the global conformational landscape of an enzyme as a mechanism for increasing catalytic activity.

biochemistry↗