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TitleStructural morphing in the viral portal vertex of bacteriophage lambda.
Journal, issue, pagesJ Virol, Vol. 98, Issue 5, Page e0006824, Year 2024
Publish dateMay 14, 2024
AuthorsZhiwei Gu / Kexun Wu / Jiawei Wang /
PubMed AbstractThe portal protein of tailed bacteriophage plays essential roles in various aspects of capsid assembly, motor assembly, genome packaging, connector formation, and infection processes. After DNA ...The portal protein of tailed bacteriophage plays essential roles in various aspects of capsid assembly, motor assembly, genome packaging, connector formation, and infection processes. After DNA packaging is complete, additional proteins are assembled onto the portal to form the connector complex, which is crucial as it bridges the mature head and tail. In this study, we report high-resolution cryo-electron microscopy (cryo-EM) structures of the portal vertex from bacteriophage lambda in both its prohead and mature virion states. Comparison of these structures shows that during head maturation, in addition to capsid expansion, the portal protein undergoes conformational changes to establish interactions with the connector proteins. Additionally, the independently assembled tail undergoes morphological alterations at its proximal end, facilitating its connection to the head-tail joining protein and resulting in the formation of a stable portal-connector-tail complex. The B-DNA molecule spirally glides through the tube, interacting with the nozzle blade region of the middle-ring connector protein. These insights elucidate a mechanism for portal maturation and DNA translocation within the phage lambda system.
IMPORTANCE: The tailed bacteriophages possess a distinct portal vertex that consists of a ring of 12 portal proteins associated with a 5-fold capsid shell. This portal protein is crucial in multiple stages of virus assembly and infection. Our research focused on examining the structures of the portal vertex in both its preliminary prohead state and the fully mature virion state of bacteriophage lambda. By analyzing these structures, we were able to understand how the portal protein undergoes conformational changes during maturation, the mechanism by which it prevents DNA from escaping, and the process of DNA spirally gliding.
External linksJ Virol / PubMed:38661364 / PubMed Central
MethodsEM (single particle)
Resolution3.32 - 5.58 Å
Structure data

38540

8xot

EMDB-38540, PDB-8xot:
Prohead portal of bacteriophage lambda
Method: EM (single particle) / Resolution: 3.51 Å

38541

8xou

EMDB-38541, PDB-8xou:
Prohead portal vertex of bacteriophage lambda
Method: EM (single particle) / Resolution: 5.58 Å

38542

8xow

EMDB-38542, PDB-8xow:
Mature virion portal of bacteriophage lambda
Method: EM (single particle) / Resolution: 3.32 Å

38556

8xpm

EMDB-38556, PDB-8xpm:
Mature virion portal of phage lambda with DNA
Method: EM (single particle) / Resolution: 3.9 Å

38572

8xqb

EMDB-38572, PDB-8xqb:
Mature virion portal vertex of bacteriophage lambda
Method: EM (single particle) / Resolution: 4.07 Å

Source
  • escherichia phage lambda (virus)
KeywordsVIRAL PROTEIN / caudovirales / siphoviridae / portal vertex / portal / capsid / connector/neck / tail / delivery device / B-DNA / phage lambda / VIRAL PROTEIN/DNA / Bacteriophage / VIRAL PROTEIN-DNA COMPLEX

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