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Palmitoylation of virus proteins
1Department of Immunology and Molecular Biology, Free University, Berlin, Germany. mveit@zedat.fu-berlin.de
Biology of the Cell
|May 3, 2012
Summary
This review covers over 30 years of research on viral protein palmitoylation (S-acylation). It details methods, biochemistry, and functional impacts of this fatty acid modification on viral pathogens like influenza.
Area of Science:
- Biochemistry
- Virology
- Molecular Biology
Background:
- Palmitoylation (S-acylation) is a post-translational modification involving fatty acid attachment to cysteine residues.
- This process is crucial for integral and peripheral membrane proteins, including those of viral pathogens.
- Understanding viral protein palmitoylation aids in characterizing cellular pathogens and deciphering cellular palmitoylation machinery.
Purpose of the Study:
- To comprehensively review over 30 years of research on the palmitoylation of viral proteins.
- To describe methods for identifying S-acylated proteins and the fundamental biochemistry of palmitoylation.
- To discuss the functional consequences of palmitoylation in viral life cycles.
Main Methods:
- Literature review of over 30 years of research.
- Analysis of established methods for identifying S-acylated proteins.
- Biochemical and functional analysis of palmitoylation in viral proteins.
Main Results:
- Palmitoylation sites, fatty acid species, and intracellular locations of palmitoylation in viral proteins are detailed.
- The enzymology of the palmitoylation reaction is covered.
- Functional consequences include protein-membrane binding, viral entry via membrane fusion, and virus assembly/release.
Conclusions:
- Palmitoylation significantly impacts viral protein function and the viral life cycle.
- This modification is essential for the infectivity and propagation of various viruses.
- Studying viral palmitoylation offers insights into both viral pathogenesis and host cell biology.
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