Pasture Forage Quality in West Virginia - 1999 to 2001

WVU-Extension fact shee

Pasture Forage Quality in West Virginia

WVU-Extension fact shee

Differential Type I Interferon Signaling Is a Master Regulator of Susceptibility to Postinfluenza Bacterial Superinfection

Bacterial superinfections are a primary cause of death during influenza pandemics and epidemics. Type I interferon (IFN) signaling contributes to increased susceptibility of mice to bacterial superinfection around day 7 post-influenza A virus (IAV) infection. Here we demonstrate that the reduced susceptibility to methicillin-resistant Staphylococcus aureus (MRSA) at day 3 post-IAV infection, which we previously reported was due to interleukin-13 (IL-13)/IFN-γ responses, is also dependent on type I IFN signaling and its subsequent requirement for protective IL-13 production. We found, through utilization of blocking antibodies, that reduced susceptibility to MRSA at day 3 post-IAV infection was IFN-β dependent, whereas the increased susceptibility at day 7 was IFN-α dependent. IFN-β signaling early in IAV infection was required for MRSA clearance, whereas IFN-α signaling late in infection was not, though it did mediate increased susceptibility to MRSA at that time. Type I IFN receptor (IFNAR) signaling in CD11c+ and Ly6G+ cells was required for the observed reduced susceptibility at day 3 post-IAV infection. Depletion of Ly6G+ cells in mice in which IFNAR signaling was either blocked or deleted indicated that Ly6G+ cells were responsible for the IFNAR signaling-dependent susceptibility to MRSA superinfection at day 7 post-IAV infection. Thus, during IAV infection, the temporal differences in type I IFN signaling increased bactericidal activity of both CD11c+ and Ly6G+ cells at day 3 and reduced effector function of Ly6G+ cells at day 7. The temporal differential outcomes induced by IFN-β (day 3) and IFN-α (day 7) signaling through the same IFNAR resulted in differential susceptibility to MRSA at 3 and 7 days post-IAV infection

Animal Production Systems for Pasture-Based Livestock Production (NRAES 171)

This 246 page publication (NRAES-171) was originally published by the Natural Resource, Agriculture, and Engineering Service (NRAES, previously known as the Northeast Regional Agricultural Engineering Service), a multi-university program in the Northeast US disbanded in 2011. Plant and Life Sciences Publishing (PALS) was subsequently formed to manage the NRAES catalog. Ceasing operations in 2018, PALS was a program of the Department of Horticulture in the College of Agriculture and Life Sciences (CALS) at Cornell University. PALS assisted university faculty in publishing, marketing and distributing books for small farmers, gardeners, land owners, workshops, college courses, and consumers.The book explores foraging behavior, basic animal nutrition, and parasite control for pasture-based animals with chapters devoted to beef, dairy, sheep, goat, and horse nutrition and management

Substituted hippurates and hippurate analogs as substrates and inhibitors of peptidylglycine a-hydroxylating monooxygenase (PHM)

Peptidyl a-hydroxylating monooxygenase (PHM) functions in vivo towards the biosynthesis of a-amidated peptide hormones in mammals and insects. PHM is a potential target for the development of inhibitors as drugs for the treatment of human disease and as insecticides for the management of insect pests. We show here that relatively simple ground state analogs of the PHM substrate hippuric acid (C6H5-CO-NH-CH2-COOH) inhibit the enzyme with Ki values as low as 0.5 µM. Substitution of sulfur atom(s) into the hippuric acid analog increases the affinity of PHM for the inhibitor. Replacement of the acetylglycine moiety, -CO-NH-CH2-COOH with an S-(thioacetyl)thioglycolic acid moiety, -CS-S-CH2-COOH, yields compounds with the highest PHM affinity. Both S-(2-phenylthioacetyl)thioglycolate and S-(4-ethylthiobenzoyl)thioglycolic acid inhibit the proliferation of cultured human prostate cancer cells at concentrations >100-fold excess of their respective Ki values. Comparison of Ki values between mammalian PHM and insect PHM shows differences in potency suggesting that a PHM-based insecticide with limited human toxicity can be developed. © 2008 Elsevier Ltd. All rights reserved

Geometric and electronic structure and reactivity of a mononuclear 'side-on' nickel(III)-peroxo complex

Metal-dioxygen adducts, such as metal-superoxo and -peroxo species, are key intermediates often detected in the catalytic cycles of dioxygen activation by metalloenzymes and biomimetic compounds. The synthesis and spectroscopic characterization of an end-on nickel(II)-superoxo complex with a 14-membered macrocyclic ligand was reported previously. Here we report the isolation, spectroscopic characterization, and high-resolution crystal structure of a mononuclear side-on nickel(III)-peroxo complex with a 12-membered macrocyclic ligand, [Ni(12-TMC)(O(2))](+) (1) (12-TMC = 1,4,7,10-tetramethyl-1,4,7,10-tetraazacyclododecane). In contrast to the end-on nickel(II)-superoxo complex, the nickel(III)-peroxo complex is not reactive in electrophilic reactions, but is capable of conducting nucleophilic reactions. The nickel(III)-peroxo complex transfers the bound dioxygen to manganese(II) complexes, thus affording the corresponding nickel(II) and manganese(III)peroxo complexes. Our results demonstrate the significance of supporting ligands in tuning the geometric and electronic structures and reactivities of metal-O(2) intermediates that have been shown to have biological as well as synthetic usefulness in biomimetic reactions