Chemical stimuli override a temperature-dependent morphological program by reprogramming the transcriptome of a fungal pathogen.

The human fungal pathogen changes its morphology in response to temperature. At 37°C, it grows as a budding yeast, whereas at room temperature (RT), it transitions to hyphal growth. Prior work has demonstrated that 15-20% of transcripts are temperature-regulated, and that transcription factors (TFs) Ryp1-4 are necessary to establish yeast growth.

Chemical stimuli override a temperature-dependent morphological program by reprogramming the transcriptome of a fungal pathogen.

Unlabelled: The human fungal pathogen changes its morphology in response to temperature. At 37°C it grows as a budding yeast whereas at room temperature it transitions to hyphal growth. Prior work has demonstrated that 15-20% of transcripts are temperature-regulated, and that transcription factors Ryp1-4 are necessary to establish yeast growth.

Mapping the Resistance Potential of Influenza's H Channel against an Antiviral Blocker.

The development of drug resistance has long plagued our efforts to curtail viral infections in general and influenza in particular. The problem is particularly challenging since the exact mode of resistance may be difficult to predict, without waiting for untreatable strains to evolve. Herein, a different approach is taken.

Bacteria-based analysis of HIV-1 Vpu channel activity.

HIV-1 Vpu is a small, single-span membrane protein with two attributed functions that increase the virus' pathogenicity: degradation of CD4 and inactivation of BST-2. Vpu has also been shown to possess ion channel activity, yet no correlation has been found between this attribute and Vpu's role in viral release. In order to gain further insight into the channel activity of Vpu we devised two bacteria-based assays that can examine this function in detail.

Computational and experimental analysis of drug binding to the Influenza M2 channel.

The Influenza Matrix 2 (M2) protein is the target of Amantadine and Rimantadine which block its H(+) channel activity. However, the potential of these aminoadamantyls to serve as anti-flu agents is marred by the rapid resistance that the virus develops against them. Herein, using a cell based assay that we developed, we identify two new aminoadamantyl derivatives that show increased activity against otherwise resistant M2 variants.