Abstract
Background Human prototypic foamy virus (HPFV) belongs to the spumaretrovrinae subfamily and is an attractive vector candidate for gene therapy [1] as it is apathogenic. The Gag protein is not cleaved into matrix (MA), capsid (CA) and nucleocapsid (NC) as occurs in orthoretroviruses; rather, it is able to perform the roles of these proteins as a single polypeptide [2]. Foamy virus Gag proteins are targets for restriction factors such as Trim5a [3] and also interact with the aminoterminal leader peptide of the envelope protein (Env). This Gag-Env interaction is essential for budding of viral particles from the host cell [4,5].
Highlights
Human prototypic foamy virus (HPFV) belongs to the spumaretrovrinae subfamily and is an attractive vector candidate for gene therapy [1] as it is apathogenic
The identification of a secondary self-association region suggests that these dimers may undergo further multimerisation in the full-length Gag protein
Comparison of Trim5a specificity between foamy viruses suggests that the recognition site resides on the exposed surface of the N-terminal domain of the Gag protein
Summary
Human prototypic foamy virus (HPFV) belongs to the spumaretrovrinae subfamily and is an attractive vector candidate for gene therapy [1] as it is apathogenic. The Gag protein is not cleaved into matrix (MA), capsid (CA) and nucleocapsid (NC) as occurs in orthoretroviruses; rather, it is able to perform the roles of these proteins as a single polypeptide [2]. Foamy virus Gag proteins are targets for restriction factors such as Trim5a [3] and interact with the aminoterminal leader peptide of the envelope protein (Env). This Gag-Env interaction is essential for budding of viral particles from the host cell [4,5].
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