Recombinant Feline foamy virus Envelope glycoprotein gp130 (env)
Description
Introduction to Recombinant Feline Foamy Virus Envelope Glycoprotein gp130 (env)
The recombinant Feline Foamy Virus (FFV) envelope glycoprotein gp130 is a crucial component of the virus, playing a pivotal role in its life cycle, particularly in viral entry and budding. Foamy viruses, part of the Retroviridae family, exhibit unique characteristics distinct from other retroviruses, including their envelope glycoprotein structure and processing. This article delves into the specifics of the recombinant FFV envelope glycoprotein gp130, its biosynthesis, structure, and functional significance.
Biosynthesis and Structure of gp130
The gp130 envelope glycoprotein precursor undergoes a complex biosynthesis process. Initially translated as a full-length precursor protein, it is processed into three subunits: the leader peptide (LP), surface (SU), and transmembrane (TM) subunits. This processing occurs post-translationally by cellular furin-like proteases during transport to the cell surface . The LP subunit is essential for viral budding and interacts with the viral capsid .
| Subunit | Function | Topology |
|---|---|---|
| LP | Essential for viral budding and capsid interaction | Type II membrane topology |
| SU | Binds to host cell receptors | Internal subunit |
| TM | Anchors the envelope complex in the viral membrane | Type I membrane topology |
Functional Significance of gp130 Subunits
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Leader Peptide (LP): The LP is crucial for particle budding and release. It interacts with the N-terminal sequences of the Gag protein, facilitating the morphogenesis of the virus .
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Surface (SU) Subunit: This subunit is responsible for binding to host cell receptors, initiating viral entry. The receptor-binding domain (RBD) of the SU subunit is essential for host cell recognition and attachment .
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Transmembrane (TM) Subunit: The TM subunit anchors the envelope complex to the viral membrane and plays a role in the fusion process during viral entry .
Research Findings on Recombinant gp130
Studies on recombinant FFV gp130 have focused on understanding its biosynthesis, structure, and function. Mutational analyses have identified critical regions within the SU subunit necessary for receptor binding and viral infectivity. For instance, N-glycosylation sites, particularly at position 391, are crucial for proper folding and function of the RBD .
References Characterization of the Prototype Foamy Virus Envelope... Characterization of the Prototype Foamy Virus Envelope... Furin-Mediated Cleavage of the Feline Foamy Virus Env Leader Protein Recombinant feline herpesviruses expressing feline leukemia virus... Analysis and Function of Prototype Foamy Virus Envelope N... Genetic and biological characterization of feline foamy virus isolated from a leopard cat (Prionailurus bengalensis) in Vietnam env - Envelope glycoprotein gp130 - Feline foamy virus (FFV) - UniProt An Endoplasmic Reticulum Retrieval Signal Partitions Human... Specific Interaction of a Novel Foamy Virus Env Leader Protein with...
Product Specs
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Target Background
The surface protein (SU) mediates viral attachment to the host cell by binding to its receptor. This interaction triggers a conformational change in the transmembrane protein (TM), activating its fusogenic properties by exposing its fusion peptide. The transmembrane protein (TM) functions as a class I viral fusion protein. Current models suggest at least three conformational states: a pre-fusion native state, a pre-hairpin intermediate state, and a post-fusion hairpin state. During membrane fusion, the coiled-coil regions (heptad repeats) form a trimer-of-hairpins structure, bringing the fusion peptide into close proximity to the C-terminal ectodomain. This structural rearrangement drives the apposition and subsequent fusion of viral and host cell membranes, delivering the nucleocapsid into the cytoplasm. The leader peptide is a component of infectious virions and is essential for particle budding.
KEGG: vg:4405350
