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TitleCryo-electron microscopy structures of capsids and in situ portals of DNA-devoid capsids of human cytomegalovirus.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 2025, Year 2023
Publish dateApr 11, 2023
AuthorsZhihai Li / Jingjing Pang / Rongchao Gao / Qingxia Wang / Maoyan Zhang / Xuekui Yu /
PubMed AbstractThe portal-scaffold complex is believed to nucleate the assembly of herpesvirus procapsids. During capsid maturation, two events occur: scaffold expulsion and DNA incorporation. The portal-scaffold ...The portal-scaffold complex is believed to nucleate the assembly of herpesvirus procapsids. During capsid maturation, two events occur: scaffold expulsion and DNA incorporation. The portal-scaffold interaction and the conformational changes that occur to the portal during the different stages of capsid formation have yet to be elucidated structurally. Here we present high-resolution structures of the A- and B-capsids and in-situ portals of human cytomegalovirus. We show that scaffolds bind to the hydrophobic cavities formed by the dimerization and Johnson-fold domains of the major capsid proteins. We further show that 12 loop-helix-loop fragments-presumably from the scaffold domain-insert into the hydrophobic pocket of the portal crown domain. The portal also undergoes significant changes both positionally and conformationally as it accompanies DNA packaging. These findings unravel the mechanism by which the portal interacts with the scaffold to nucleate capsid assembly and further our understanding of scaffold expulsion and DNA incorporation.
External linksNat Commun / PubMed:37041152 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 9.3 Å
Structure data

EMDB-34691: C5 portal vertex in HCMV A-capsid
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-34692, PDB-8heu:
C12 portal in HCMV A-capsid
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-34693, PDB-8hev:
C12 portal in HCMV B-capsid
Method: EM (single particle) / Resolution: 4.2 Å

EMDB-34694: C1 portal vertex in HCMV A-capsid
Method: EM (single particle) / Resolution: 5.1 Å

EMDB-34695: Asymmetric reconstruction of HCMV A-capsid
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-34696, PDB-8hex:
C5 portal vertex in HCMV B-capsid
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-34697: C1 portal vertex in HCMV B-capsid
Method: EM (single particle) / Resolution: 4.8 Å

EMDB-34698: Icosahedral reconstruction of HCMV A-capsid
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-34699: Icosahedral recontruction of HCMV B-capsid
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-34700: Asymmetric reconstruction of HCMV B-capsid
Method: EM (single particle) / Resolution: 7.2 Å

EMDB-34701: C5 portal vertex in NIEPs capsid of HCMV
Method: EM (single particle) / Resolution: 5.0 Å

EMDB-34702: C12 portal in NIEPs capsid of HCMV
Method: EM (single particle) / Resolution: 6.9 Å

EMDB-34703: Asymmetric reconstruction of portal vertex in NIEPs capsid of HCMV
Method: EM (single particle) / Resolution: 7.3 Å

EMDB-34704, PDB-8hey:
One CVSC-binding penton vertex in HCMV B-capsid
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-34706: Asymmetric reconstruction of NIEPs capsid in HCMV
Method: EM (single particle) / Resolution: 9.3 Å

Source
  • human herpesvirus 5 strain ad169
  • human betaherpesvirus 5
KeywordsVIRAL PROTEIN / A-capsid / portal / in-situ structure / VIRUS / B-capsid / C5 portal vertex / one CVSC-binding penton vertex / asymmetric reconstruction

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