Publications by authors named "Eric Gillitzer"

Article Synopsis
  • - Fuselloviridae are viruses that thrive in high-temperature, acidic hot springs globally, with SSV1 being the most studied type, featuring a double-stranded DNA genome with 34 open reading frames.
  • - Researchers studied the F112 protein from SSV1 and found it to be a monomeric intracellular protein with a unique DNA-binding structure that includes an intrachain disulfide bond.
  • - The study highlights the presence of disulfide bonds in proteins from hyperthermophilic viruses and shows lower cysteine levels in membrane proteins of these viruses, leading to discussions on the evolutionary implications of SSV1's distribution.
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Protein cage nanoparticles have the potential to serve as multifunctional cell targeted, imaging and therapeutic platforms for broad applications in medicine. However, before they find applications in medicine, their biocompatibility in vivo needs to be demonstrated. We provide here baseline biodistribution information of two different spherical protein cage nanoplatforms, the 28 nm viral Cowpea chlorotic mottle virus (CCMV) and the 12 nm heat shock protein (Hsp) cage.

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The selectivity of antimicrobial photodynamic therapy (PDT) can be enhanced by coupling the photosensitizer (PS) to a targeting ligand. Nanoplatforms provide a medium for designing delivery vehicles that incorporate both functional attributes. We report here the photodynamic inactivation of a pathogenic bacterium, Staphylococcus aureus, using targeted nanoplatforms conjugated to a photosensitizer (PS).

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Of the three domains of life (Eukarya, Bacteria, and Archaea), the least understood is Archaea and its associated viruses. Many Archaea are extremophiles, with species that are capable of growth at some of the highest temperatures and extremes of pH of all known organisms. Phylogenetic rRNA-encoding DNA analysis places many of the hyperthermophilic Archaea (species with an optimum growth > or = 80 degrees C) at the base of the universal tree of life, suggesting that thermophiles were among the first forms of life on earth.

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Here we present generalized methods for chemically modifying the surface of a viral protein cage; this exploits the chemistry of native and engineered surface exposed functional groups for multivalent presentation of ligands.

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