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TitleMolecular Architecture of Salmonella Typhimurium Virus P22 Genome Ejection Machinery.
Journal, issue, pagesJ Mol Biol, Vol. 435, Issue 24, Page 168365, Year 2023
Publish dateDec 15, 2023
AuthorsStephano M Iglesias / Ravi K Lokareddy / Ruoyu Yang / Fenglin Li / Daniel P Yeggoni / Chun-Feng David Hou / Makayla N Leroux / Juliana R Cortines / Justin C Leavitt / Mary Bird / Sherwood R Casjens / Simon White / Carolyn M Teschke / Gino Cingolani /
PubMed AbstractBacteriophage P22 is a prototypical member of the Podoviridae superfamily. Since its discovery in 1952, P22 has become a paradigm for phage transduction and a model for icosahedral viral capsid ...Bacteriophage P22 is a prototypical member of the Podoviridae superfamily. Since its discovery in 1952, P22 has become a paradigm for phage transduction and a model for icosahedral viral capsid assembly. Here, we describe the complete architecture of the P22 tail apparatus (gp1, gp4, gp10, gp9, and gp26) and the potential location and organization of P22 ejection proteins (gp7, gp20, and gp16), determined using cryo-EM localized reconstruction, genetic knockouts, and biochemical analysis. We found that the tail apparatus exists in two equivalent conformations, rotated by ∼6° relative to the capsid. Portal protomers make unique contacts with coat subunits in both conformations, explaining the 12:5 symmetry mismatch. The tail assembles around the hexameric tail hub (gp10), which folds into an interrupted β-propeller characterized by an apical insertion domain. The tail hub connects proximally to the dodecameric portal protein and head-to-tail adapter (gp4), distally to the trimeric tail needle (gp26), and laterally to six trimeric tailspikes (gp9) that attach asymmetrically to gp10 insertion domain. Cryo-EM analysis of P22 mutants lacking the ejection proteins gp7 or gp20 and biochemical analysis of purified recombinant proteins suggest that gp7 and gp20 form a molecular complex associated with the tail apparatus via the portal protein barrel. We identified a putative signal transduction pathway from the tailspike to the tail needle, mediated by three flexible loops in the tail hub, that explains how lipopolysaccharide (LPS) is sufficient to trigger the ejection of the P22 DNA in vitro.
External linksJ Mol Biol / PubMed:37952769 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.4 Å
Structure data

41649

8tvr

EMDB-41649: P22 Mature Virion tail - C6 Localized Reconstruction
PDB-8tvr: In situ cryo-EM structure of bacteriophage P22 tail hub protein: tailspike protein complex at 2.8A resolution
Method: EM (single particle) / Resolution: 2.8 Å

41651

8tvu

EMDB-41651, PDB-8tvu:
In situ cryo-EM structure of bacteriophage P22 portal protein: head-to-tail protein complex at 3.0A resolution
Method: EM (single particle) / Resolution: 3.0 Å

41791

8u10

EMDB-41791, PDB-8u10:
In situ cryo-EM structure of bacteriophage P22 gp1:gp4:gp5:gp10:gp9 N-term complex in conformation 1 at 3.2A resolution
Method: EM (single particle) / Resolution: 3.2 Å

41792

8u11

EMDB-41792, PDB-8u11:
In situ cryo-EM structure of bacteriophage P22 gp1:gp5:gp4: gp10: gp9 N-term complex in conformation 2 at 3.1A resolution
Method: EM (single particle) / Resolution: 3.1 Å

41819

8u1o

EMDB-41819, PDB-8u1o:
In situ cryo-EM structure of bacteriophage P22 tailspike protein complex at 3.4A resolution
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • salmonella phage p22 (virus)
KeywordsVIRAL PROTEIN / phage / bacteriophage / tail spike protein / TSP / gene product 9 (gp9) / Packaged DNA stabilization protein / gene product 10 (gp10) / STRUCTURAL PROTEIN / portal protein / head-to-tail protein / gene product 1 (gp1) / gene product 4 (gp4 / gene product 4 (gp4) / Tail hub protein / gene product (1) / Coat protein / Major capsid protein / gene product 5 (gp5) / Tailspike protein

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