Current address: Laboratory of Cell Biology, NCI Bethesda, Bethesda, MD, USA.
Characterization of the Effects of Aryl-azido Compounds and UVA Irradiation on the Viral Proteins and Infectivity of Human Immunodeficiency Virus Type 1
Article first published online: 7 SEP 2010
© 2010 U.S. Government. Journal Compilation. The American Society of Photobiology
Photochemistry and Photobiology
Volume 86, Issue 5, pages 1099–1108, September/October 2010
How to Cite
Belanger, J. M., Raviv, Y., Viard, M., Jason de la Cruz, M., Nagashima, K. and Blumenthal, R. (2010), Characterization of the Effects of Aryl-azido Compounds and UVA Irradiation on the Viral Proteins and Infectivity of Human Immunodeficiency Virus Type 1. Photochemistry and Photobiology, 86: 1099–1108. doi: 10.1111/j.1751-1097.2010.00780.x
- Issue published online: 7 SEP 2010
- Article first published online: 7 SEP 2010
- Received 15 March 2010, accepted 27 May 2010
Hydrophobic UV-activatable compounds have been shown to partition into the hydrophobic region of biological membranes to selectively label transmembrane proteins, and to inactivate enveloped viruses. Here, we analyze various UV-activatable azido- and iodo-based hydrophobic compounds for their ability to inactivate a model-enveloped virus, human immunodeficiency virus (HIV-1 MN). Treatment of HIV-1 with 1,5-diazidonapthalene (DAN), 1-iodo, 5-azidonaphthalene (INA), 1-azidonaphthalene (AzNAP) or 4,4′-diazidobiphenyl (DABIPH) followed by UVA irradiation for 2 min resulted in complete viral inactivation, whereas treatment using analogous non–azido-containing controls had no effect. Incorporation of an azido moiety within these hydrophobic compounds to promote photoinduced covalent reactions with proteins was found to be the primary mechanism of viral inactivation for this class of compounds. Prolonged UVA irradiation of the virus in the presence of these azido compounds resulted in further modifications of viral proteins, due to the generation of reactive oxygen species, leading to aggregation as visualized via Western blot analysis, providing additional viral modifications that may inhibit viral infectivity. Furthermore, inactivation using these compounds resulted in the preservation of surface antigenic structures (recognized by neutralizing antibodies b12, 2g12 and 4e10), which is favorable for the creation of vaccines from these inactivated virus preparations.