Putting drug resistant epithelial herpes keratitis in the spotlight: A case series.

Purpose: To strengthen the sparse evidence on acyclovir (ACV) resistance, especially in recalcitrant herpetic keratitis (HK), by describing the clinical course of 3 genotypically proven ACV resistant HK cases. An overview of mechanisms of resistance and therapeutic options currently available to ophthalmologists is provided based upon recent literature search.

Observations: Resistance to ACV due to known mutations in the gene encoding the viral thymidine kinase was confirmed in 2 cases, and a novel mutation in the UL23 gene (N202K) conferring phenotypical resistance to ACV was discovered in 1 case.

On the Role of Additional [4Fe-4S] Clusters with a Free Coordination Site in Radical-SAM Enzymes.

The canonical CysXXXCysXXCys motif is the hallmark of the Radical-SAM superfamily. This motif is responsible for the ligation of a [4Fe-4S] cluster containing a free coordination site available for SAM binding. The five enzymes MoaA, TYW1, MiaB, RimO and LipA contain in addition a second [4Fe-4S] cluster itself bound to three other cysteines and thus also displaying a potentially free coordination site.

Impact of Surgical Technique on Long-term Complication Rate After Laparoscopic Adjustable Gastric Banding (LAGB): Results of a Single-blinded Randomized Controlled trial (ANOSEAN Study).

Objective: The aim of the study was to explore the impact of the absence of band fixation on the reoperation rate and to identify other risk factors for long-term complications.

Background: Laparoscopic adjustable gastric banding has been demonstrated to permit important weight loss and comorbidity improvement, but some bands will have to be removed mainly for failure or in case of planned 2-step surgery. Then, the absence of a gastro-gastric suture (GGS) would allow easier band removal.

Redox Behavior of the S-Adenosylmethionine (SAM)-Binding Fe-S Cluster in Methylthiotransferase RimO, toward Understanding Dual SAM Activity.

RimO, a radical-S-adenosylmethionine (SAM) enzyme, catalyzes the specific C methylthiolation of the D89 residue in the ribosomal S protein. Two intact iron-sulfur clusters and two SAM cofactors both are required for catalysis. By using electron paramagnetic resonance, Mössbauer spectroscopies, and site-directed mutagenesis, we show how two SAM molecules sequentially bind to the unique iron site of the radical-SAM cluster for two distinct chemical reactions in RimO.