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Lysine addressability and mammalian cell interactions of bacteriophage lambda procapsids

Citation:

Koudelka KJ, Ippoliti S, Medina E, Shriver LP, Trauger SA, Catalano CE, Manchester M. Lysine addressability and mammalian cell interactions of bacteriophage lambda procapsids. BiomacromoleculesBiomacromoleculesBiomacromolecules. 2013;14 :4169-76.

Date Published:

Dec 9

Abstract:

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 lambda was studied for its lysine addressability, stability, cellular uptake, and the ability to modify its cellular uptake. lambda 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 lambda procapsids and their potential use as targeted drug delivery vehicles.

Notes:

Koudelka, Kristopher JIppoliti, ShannonMedina, ElizabethShriver, Leah PTrauger, Sunia ACatalano, Carlos EManchester, MarianneCA112075/CA/NCI NIH HHS/Biomacromolecules. 2013 Dec 9;14(12):4169-76. doi: 10.1021/bm401577f. Epub 2013 Nov 26.