Abstract
Background We have recently demonstrated that under highly artificial conditions, retroviral envelopes can acquire new proteins carrying a post-translationally added glycosylphosphatidylinositol (GPI) anchor [1,2]. Subsequently, we are interested to see if retroviral particles may acquire novel protein functions post-exit under physiological conditions either using GPI-anchored or, eventually, other protein species. Therefore we are trying to assess how mutable the envelope proteome is in response to external stimuli. New functionalities acquired in such processes, i.e. protection from the complement system, may prove beneficial for the virus, especially in zoonotic infections.
Highlights
We have recently demonstrated that under highly artificial conditions, retroviral envelopes can acquire new proteins carrying a post-translationally added glycosylphosphatidylinositol (GPI) anchor [1,2]
When GPI anchored mGFP, CD59, or IL2 were added to lenti-viral vector particles, the respective functions could be conferred to the vector particles
We have found that high protein backgrounds are permissive for insertion of low-abundance GPI anchored proteins and that protein functions are transferable with potential benefits for the virus
Summary
We have recently demonstrated that under highly artificial conditions, retroviral envelopes can acquire new proteins carrying a post-translationally added glycosylphosphatidylinositol (GPI) anchor [1,2]. Were used, association of GPI anchored proteins is still possible.
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