Two- and Three-Dimensional Bioengineered Human Intestinal Tissue Models for Cryptosporidium.

Conventional cell cultures utilizing transformed or immortalized cell lines or primary human epithelial cells have played a fundamental role in furthering our understanding of Cryptosporidium infection. However, they remain inadequate with respect to their inability to emulate in vivo conditions, support long-term growth, and complete the life cycle of the parasite. Previously, we developed a 3D silk scaffold-based model using transformed human intestinal epithelial cells (IECs).

Disruption of the Putative Ribosome-Binding Motif of a Scaffold Protein Impairs Cytochrome Oxidase Subunit Expression in .

During their parasitic life cycle, through sandflies and vertebrate hosts, parasites confront strikingly different environments, including abrupt changes in pH and temperature, to which they must rapidly adapt. These adaptations include alterations in gene expression, metabolism, and morphology, allowing them to thrive as promastigotes in the sandfly and as intracellular amastigotes in the vertebrate host. A critical aspect of metabolic adaptation to these changes is maintenance of efficient mitochondrial function in the hostile vertebrate environment.

Recent Breakthroughs and Ongoing Limitations in Research.

The intestinal apicomplexan parasite is a major cause of diarrheal disease in humans worldwide. However, treatment options are severely limited. The search for novel interventions is imperative, yet there are several challenges to drug development, including intractability of the parasite and limited technical tools to study it.

LACK, a RACK1 ortholog, facilitates cytochrome c oxidase subunit expression to promote Leishmania major fitness.

Leishmania are kinetoplastid parasites that cause the sandfly-transmitted disease leishmaniasis. To maintain fitness throughout their infectious life cycle, Leishmania must undergo rapid metabolic adaptations to the dramatically distinct environments encountered during transition between sandfly and vertebrate hosts. We performed proteomic and immunoblot analyses of attenuated L.

Epidermal growth factor stimulates extracellular-signal regulated kinase phosphorylation of a novel site on cytoplasmic Dynein intermediate chain 2.

Extracellular-signal regulated kinase (ERK) signaling is required for a multitude of physiological and patho-physiological processes. However, the identities of the proteins that ERK phosphorylates to elicit these responses are incompletely known. Using an affinity purification methodology of general utility, here we identify cytoplasmic dynein intermediate chain 2 (DYNC1I-2, IC-2) as a novel substrate for ERK following epidermal growth factor receptor stimulation of fibroblasts.