A lipid modified ubiquitin is packaged into particles of several enveloped viruses

0Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

Abstract

An anti-ubiquitin cross-reactive protein which migrates more slowly (6.5 kDa) by SDS-PAGE than ubiquitin was identified in African swine fever virus particles. This protein was extracted into the detergent phase in Triton X-114 phase separations, showing that it is hydrophobic, and was radiolabelled with both [3H]palmitic acid and [32P]orthophosphate. This indicates that the protein has a similar structure to the membrane associated phosphatidyl ubiquitin described in baculovirus particles. A similar molecule was found in vaccinia virus and herpes simplex virus particles, suggesting that it may be a component of uninfected cell membranes, which is incorporated into membrane layers in virions during morphogenesis.

Author supplied keywords

Cite

CITATION STYLE

APA

Webb, J. H., Mayer, R. J., & Dixon, L. K. (1999). A lipid modified ubiquitin is packaged into particles of several enveloped viruses. FEBS Letters, 444(1), 136–139. https://doi.org/10.1016/S0014-5793(99)00025-3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free