Presentation Title

Effects of site-directed mutagenesis on STIV’s major capsid protein on ESCRT recruitment.

Faculty Mentor

Jamie C Snyder

Start Date

23-11-2019 10:45 AM

End Date

23-11-2019 11:30 AM

Location

86

Session

poster 4

Type of Presentation

Poster

Subject Area

biological_agricultural_sciences

Abstract

Sulfolobus turreted icosahedral virus (STIV) is an archaeal virus that infects Sulfolobus solfataricus. Although it has emerged as a model archaeal virus, its replication cycle has not been fully characterized. However, we have found that STIV exploits the Endosomal Sorting Complex Required for Transport (ESCRT) machinery of S. solfataricus in a similar fashion to the enveloped eukaryotic viruses, HIV and HCV. This finding suggests an evolutionary link between eukaryotic and archaeal viruses. Previous studies have shown that the Major Capsid Protein (MCP) of STIV (B345) interacts with an ESCRT-III homolog (SSO0619) in the Sulfolobus genome. This interaction was eliminated when the C-terminal 22 amino acids of B345 were deleted. We hypothesize that B345 interacts with ESCRT-III (SSO0619), such that it recruits the ESCRT-III protein to vesicles that will eventually become the internal membrane of the assembled virion. This project aims to determine the specific amino acids in the C-terminus of B345 that are required for the interaction with ESCRT-III. Mutations within the C-terminal tail of B345 will be created, specifically at residues that were found to be critical to STIV's interaction with ESCRT. These constructs will be tested in context of virus replication, B345 alone (in the absence of other viral proteins) in S. solfataricus cultures, and in co-immunoprecipitation assays.

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Nov 23rd, 10:45 AM Nov 23rd, 11:30 AM

Effects of site-directed mutagenesis on STIV’s major capsid protein on ESCRT recruitment.

86

Sulfolobus turreted icosahedral virus (STIV) is an archaeal virus that infects Sulfolobus solfataricus. Although it has emerged as a model archaeal virus, its replication cycle has not been fully characterized. However, we have found that STIV exploits the Endosomal Sorting Complex Required for Transport (ESCRT) machinery of S. solfataricus in a similar fashion to the enveloped eukaryotic viruses, HIV and HCV. This finding suggests an evolutionary link between eukaryotic and archaeal viruses. Previous studies have shown that the Major Capsid Protein (MCP) of STIV (B345) interacts with an ESCRT-III homolog (SSO0619) in the Sulfolobus genome. This interaction was eliminated when the C-terminal 22 amino acids of B345 were deleted. We hypothesize that B345 interacts with ESCRT-III (SSO0619), such that it recruits the ESCRT-III protein to vesicles that will eventually become the internal membrane of the assembled virion. This project aims to determine the specific amino acids in the C-terminus of B345 that are required for the interaction with ESCRT-III. Mutations within the C-terminal tail of B345 will be created, specifically at residues that were found to be critical to STIV's interaction with ESCRT. These constructs will be tested in context of virus replication, B345 alone (in the absence of other viral proteins) in S. solfataricus cultures, and in co-immunoprecipitation assays.