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Journal article
Interactions between Hepatitis Delta Virus Proteins
Journal of virology, v 74(12), pp 5509-5515
01 Jun 2000
PMID: 10823856
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
ABSTRACT
The 195- and 214-amino-acid (aa) forms of the delta protein (δAg-S and δAg-L, respectively) of hepatitis delta virus (HDV) differ only in the 19-aa C-terminal extension unique to δAg-L. δAg-S is needed for genome replication, while δAg-L is needed for particle assembly. These proteins share a region at aa 12 to 60, which mediates protein-protein interactions essential for HDV replication. H. Zuccola et al. (Structure 6:821–830, 1998) reported a crystal structure for a peptide spanning this region which demonstrates an antiparallel coiled-coil dimer interaction with the potential to form tetramers of dimers. Our studies tested whether predictions based on this structure could be extrapolated to conditions where the peptide was replaced by full-length δAg-S or δAg-L, and when the assays were not in vitro but in vivo. Nine amino acids that are conserved between several isolates of HDV and predicted to be important in multimerization were mutated to alanine on both δAg-S and δAg-L. We found that the predicted hierarchy of importance of these nine mutations correlated to a significant extent with the observed in vivo effects on the ability of these proteins to (i) support in
trans
the replication of the HDV genome when expressed on δAg-S and (ii) act as dominant-negative inhibitors of replication when expressed on δAg-L. We thus infer that these biological activities of δAg depend on ordered protein-protein interactions.
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Details
- Title
- Interactions between Hepatitis Delta Virus Proteins
- Creators
- Gloria Moraleda - Fox Chase Cancer CenterKate Dingle - Fox Chase Cancer CenterPreetha Biswas - Fox Chase Cancer CenterJinhong Chang - Fox Chase Cancer CenterHarmon Zuccola - Harvard UniversityJames Hogle - Harvard UniversityJohn Taylor - Fox Chase Cancer Center
- Publication Details
- Journal of virology, v 74(12), pp 5509-5515
- Publisher
- American Society for Microbiology (ASM)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Microbiology and Immunology
- Web of Science ID
- WOS:000087240700014
- Scopus ID
- 2-s2.0-0034034274
- Other Identifier
- 991020547437104721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Virology