Lysine Addressability and Mammalian Cell Interactions of Bacteriophage λ Procapsids

Chemically or genetically modified virus particles, termed viral nanoparticles (VNPs), are being explored in applications such as drug delivery, vaccine development, and materials science. Each virus platform has inherent properties and advantages based on its structure, molecular composition, and biomolecular interactions. Bacteriophage λ was studied for its lysine addressability, stability, cellular uptake, and the ability to modify its cellular uptake. λ procapsids could be labeled primarily at a single residue on the gpE capsid protein as determined by tandem mass spectrometry, providing a unique attachment site for further capsid modification. Bioconjugation of transferrin to the procapsids mediated specific interaction with transferrin receptor-expressing cells. These studies demonstrate the utility of bacteriophage λ procapsids and their potential use as targeted drug delivery vehicles

McGuganetal2016_XCMSoutput

Mass Spectrometry data was analyzed using XCMS. The output from this XCMS analysis is in "McGuganetal_2016_XCMSoutput.xlsx" and contains information on feature mass to charge ratio (m/z), retention times, statistical comparisons between frog populations using an ANOVA, and relative abundance measurements for each feature in each sample

Mite LCMS data

Liquid chromatography/mass spectrometry data from mites isolated from the stomachs of Little Devil poison frogs (Oophaga sylvatica) collected from three populations in northwestern Ecuado

frog skin GCMS data

Gas chromatography/mass spectrometry data from the skin of the Little Devil frog, Oophaga sylvatica. Frogs were collected from three populations in northwest Ecuador. Dorsal skin was isolated and alkaloids were extracted with methanol

Ant LCMS data

Liquid chromatography/mass spectrometry data from ants collected in the stomachs of Little Devil frogs in three separate populations in northwest Ecuador