Identification of an ER retrieval signal in a retroviral glycoprotein
Article Abstract:
A study of a foamy virus glycoprotein sequence for the presence of known intracellular compartment retention/retrieval motifs reveals the presence of a dilysine endoplasmic reticulum (ER) retrieval signal at the cytoplasmic carboxyl termini. These proteins are resident in the ER and possess short amino acid sequence motifs that result in their localization in the ER by retrieval, retention or both. The preservation of this well characterized ER localization signal within the glycoproteins of foamy virus indicates that they satisfy a critical function in the foamy virus biology.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Point mutations are associated with a gene duplication leading to the bloodstream reexpression of a trypanosome metacylcic VSG
Article Abstract:
The final developmental stage of the African trypanosome is characterized by a restricted expression in the salivary gland of variant surface glycoproteins (VSGs) to a subset containing 10 to 20 metacyclic variant antigen types (MVATs). A bloodstream trypanosome clone expressing an MVAT VSG gene was isolated and characterized. The results showed that bloodstream reexpression of this VSG gene is associated with a gene conversion event characterized by multiple point mutations. These mutations can further contribute to trypanosome diversity.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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Budding of rabies virus particles in the absence of the spike glycoprotein
Article Abstract:
The presence of transmembrane spike proteins is required for the release of enveloped viruses from an infected cell's membranes. These membrane proteins are needed because their interaction with cytoplasmic virus components must take place before budding can occur. This process of rhabdovirus budding, which is similar to exocytotic budding, can be explored using rabies virus mutants that lack the glycoprotein G. Results indicate that rhabdovirus budding is accomplished by the coordinated and efficient action of spike and core proteins.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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