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  1. Home
  3. Structure-based Design Of A Soluble Human Cytomegalovirus Glycoprotein B Antigen Stabilized In A Prefusion-like Conformation.
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  3. Structure-based Design Of A Soluble Human Cytomegalovirus Glycoprotein B Antigen Stabilized In A Prefusion-like Conformation.

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Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like

Madeline R Sponholtz1, Patrick O Byrne1, Alison G Lee1

  • 1Department of Molecular Biosciences, The University of Texas at Austin, Austin, TX 78712.

Proceedings of the National Academy of Sciences of the United States of America
|September 4, 2024

View abstract on PubMed

Summary
This summary is machine-generated.

Researchers stabilized human cytomegalovirus glycoprotein B (gB) in its prefusion state using structure-based design. This stabilization offers new strategies for developing effective HCMV vaccines and understanding antibody responses against gB.

Keywords:
cryo-EMcytomegalovirusherpesvirusvaccine

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Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Human cytomegalovirus (HCMV) glycoprotein B (gB) is crucial for viral entry.
  • Current HCMV vaccine candidates show limited efficacy, highlighting the need for improved vaccine strategies.

Purpose of the Study:

  • To stabilize the metastable prefusion conformation of HCMV gB using structure-based design.
  • To characterize the structural and immunological properties of stabilized gB variants.

Main Methods:

  • Structure-based design to engineer amino acid substitutions in gB.
  • Cryoelectron microscopy to determine the structure of a stabilized gB variant (gB-C7).
  • Immunization of mice with soluble gB proteins (prefusion-stabilized and postfusion) to assess antibody responses.

Main Results:

  • Engineered variant gB-C7 exhibited increased expression and thermostability, adopting a prefusion-like conformation.
  • Cryo-EM revealed additional structural features at the membrane-distal apex of gB-C7.
  • Mice immunized with prefusion-stabilized or postfusion gB showed comparable neutralizing antibody titers against an HCMV laboratory strain.

Conclusions:

  • Developed strategies for stabilizing class III viral fusion proteins like HCMV gB.
  • Provided tools for further investigation of gB-directed antibody responses.
  • Findings contribute to the development of improved HCMV vaccines.