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1 July 2004 Virus Particles Monitored by Fluorescence Spectroscopy: A Potential Detection Assay for Macromolecular Assembly
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Abstract

Native fluorescence spectroscopy was used for in situ investigations of two lipid-containing bacteriophages from the cystovirus family as well as their Pseudomonad host cells. Both the viruses ϕ6 and ϕ12 and their bacterial host proteins contain the amino acid tryptophan (trp), which is the predominant fluorophore in UV. Within proteins, trp's structural environment differs, and the differences are reflected in their spectroscopic signatures. It was observed that the peak of the trp emission from both viruses was at 330 nm, a significantly shorter wavelength than trp in either the Pseudomonad host cells or the amino acid's chemical form. This allowed us to monitor the viral attachment process and subsequent lytic release of progeny virus particles by measurement of the trp emission spectra during the infection process. This work demonstrates that fluorescence may offer a novel tool to detect viruses and monitor viral infection of cells and may be part of a biodefense application.

Alexandra Alimova, A. Katz, Rakhi Podder, Glenn Minko, Hui Wei, R. R. Alfano, and Paul Gottlieb "Virus Particles Monitored by Fluorescence Spectroscopy: A Potential Detection Assay for Macromolecular Assembly," Photochemistry and Photobiology 80(1), 41-46, (1 July 2004). https://doi.org/10.1562/2004-02-11-RA-080.1
Received: 11 February 2004; Accepted: 1 April 2004; Published: 1 July 2004
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