Evidence map›Paper›PMID 42526586›Full record

ArticleJournal of molecular biology2026

Formation and Role of the Portal of Staphylococcus aureus Bacteriophage 80α.

Amarshi Mukherjee, James L Kizziah, Laura K Parker, Patrick M Lindstrom, Nehaal Akavaram, Terje Dokland

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Article in Journal of molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Amarshi MukherjeeDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
James L KizziahDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Laura K ParkerDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA; Environmental Health and Safety Services, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Patrick M LindstromDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Nehaal AkavaramDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA.
Terje DoklandDepartment of Microbiology, The University of Alabama at Birmingham, Birmingham, AL 35294, USA. Electronic address: dokland@uab.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteriophages play an important role in the pathogenicity of Staphylococcus aureus, an important human pathogen. Phages are involved in generalized and specialized transduction as well as a more specific process by which they mobilize elements known as phage-inducible chromosomal islands, of which S. aureus pathogenicity islands (SaPIs) are an important group. SaPIs are mobilized and packaged into virions made by structural proteins encoded by "helper" bacteriophages, such as 80α. The portal is a dodecameric ring located at a fivefold vertex of the phage capsid that serves multiple functions, including capsid assembly, DNA entry and exit, recruitment of ejection proteins, and tail attachment. We previously showed that portal protein expressed in E. coli forms tridecameric rings, while portals found in virions are always dodecamers. Here, we show that portals assembled at low temperature form unclosed rings that may represent portal assembly intermediates. By analyzing portal protein deletion mutants, we demonstrate the involvement of the different functional domains in phage assembly and protein incorporation.

Indexed as

Capsid ProteinsStaphylococcus aureusStaphylococcus PhagesCapsidEscherichia coliGenomic IslandsVirionVirus AssemblyCapsid Proteinsbacteriophage assemblycapsid structurecryo-electron microscopyDNA packaginggenetic mobilization

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.