Presentation Type

Oral Presentation

Start Date

5-8-2024 1:00 PM

End Date

5-8-2024 3:00 PM

Subjects

virology, extremophile, mutagenesis

Advisor

Kenneth Stedman

Student Level

Undergraduate

Abstract

The tail of Saccharolobus spindle-shaped virus 1 (SSV1) has long been thought to be composed of viral protein 4 (VP4), but recent SSV1 virion structural studies have implicated additional structural proteins C166 and B78 in SSV1’s unique tail. The exact locations of these proteins have not been confirmed. Structural proteins VP4 (C-terminus) and B78 are hypothesized to contribute to the adaptor region bridging the viral capsid to the tail, whereas C166 is thought to comprise the majority of the internal extended structure, respectively. The structural proteins comprising SSV1 lack cysteine residues. Mutations were made in the open reading frames of these proteins via site-directed mutagenesis in order to introduce cysteine residues at regions of interest in C166 and B78 selected via AlphaFold prediction. These residues allow binding of cysteine-specific nanogold particles at these sites, thus allowing precise localization of the proteins on the SSV1 virion. Results of this project will elicit a better understanding of how these proteins are present in SSV1’s tail structure and contribute to its astonishing thermoacidophilic stability.

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Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

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May 8th, 1:00 PM May 8th, 3:00 PM

Hell’s Tails: Localizing The Tail Proteins Of The Hyperthermophilic-Infecting Virus SSV1

The tail of Saccharolobus spindle-shaped virus 1 (SSV1) has long been thought to be composed of viral protein 4 (VP4), but recent SSV1 virion structural studies have implicated additional structural proteins C166 and B78 in SSV1’s unique tail. The exact locations of these proteins have not been confirmed. Structural proteins VP4 (C-terminus) and B78 are hypothesized to contribute to the adaptor region bridging the viral capsid to the tail, whereas C166 is thought to comprise the majority of the internal extended structure, respectively. The structural proteins comprising SSV1 lack cysteine residues. Mutations were made in the open reading frames of these proteins via site-directed mutagenesis in order to introduce cysteine residues at regions of interest in C166 and B78 selected via AlphaFold prediction. These residues allow binding of cysteine-specific nanogold particles at these sites, thus allowing precise localization of the proteins on the SSV1 virion. Results of this project will elicit a better understanding of how these proteins are present in SSV1’s tail structure and contribute to its astonishing thermoacidophilic stability.