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  The Molecular Mechanism of Cellular Attachment for an Archaeal Virus

Hartman, R., Eilers, B. J., Bollschweiler, D., Munson-McGee, J. H., Engelhardt, H., Young, M. J., et al. (2019). The Molecular Mechanism of Cellular Attachment for an Archaeal Virus. STRUCTURE, 27(11), 1634-1646.e3. doi:10.1016/j.str.2019.09.005.

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 Creators:
Hartman, Ross1, Author
Eilers, Brian J.1, Author
Bollschweiler, Daniel2, Author              
Munson-McGee, Jacob H.1, Author
Engelhardt, Harald2, Author              
Young, Mark J.1, Author
Lawrence, C. Martin1, Author
Affiliations:
1external, ou_persistent22              
2Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: TURRETED ICOSAHEDRAL VIRUS; SULFOLOBUS-SOLFATARICUS; CRYSTAL-STRUCTURE; ATOMIC-STRUCTURE; PROTEIN; MEMBRANE; RECEPTOR; ARCHITECTURE; BACTERIAL; SURFACEBiochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: Sulfolobus turreted icosahedral virus (STIV) is a model archaeal virus and member of the PRD1-adenovirus lineage. Although STIV employs pyramidal lysis structures to exit the host, knowledge of the viral entry process is lacking. We therefore initiated studies on STIV attachment and entry. Negative stain and cryoelectron micrographs showed virion attachment to pili-like structures emanating from the Sulfolobus host. Tomographic reconstruction and sub-tomogram averaging revealed pili recognition by the STIV C381 turret protein. Specifically, the triple jelly roll structure of C381 determined by X-ray crystallography shows that pilus recognition is mediated by conserved surface residues in the second and third domains. In addition, the STIV petal protein (C557), when present, occludes the pili binding site, suggesting that it functions as a maturation protein. Combined, these results demonstrate a role for the namesake STIV turrets in initial cellular attachment and provide the first molecular model for viral attachment in the archaeal domain of life.

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Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000494979900005
DOI: 10.1016/j.str.2019.09.005
 Degree: -

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Title: STRUCTURE
Source Genre: Journal
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Publ. Info: 50 HAMPSHIRE ST, FLOOR 5, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 27 (11) Sequence Number: - Start / End Page: 1634 - 1646.e3 Identifier: ISSN: 0969-2126