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TitleAntigenic Characterization of the HCMV gH/gL/gO and Pentamer Cell Entry Complexes Reveals Binding Sites for Potently Neutralizing Human Antibodies.
Journal, issue, pagesPLoS Pathog, Vol. 11, Issue 10, Page e1005230, Year 2015
Publish dateOct 20, 2015
AuthorsClaudio Ciferri / Sumana Chandramouli / Alexander Leitner / Danilo Donnarumma / Michael A Cianfrocco / Rachel Gerrein / Kristian Friedrich / Yukti Aggarwal / Giuseppe Palladino / Ruedi Aebersold / Nathalie Norais / Ethan C Settembre / Andrea Carfi /
PubMed AbstractHuman Cytomegalovirus (HCMV) is a major cause of morbidity and mortality in transplant patients and in fetuses following congenital infection. The glycoprotein complexes gH/gL/gO and ...Human Cytomegalovirus (HCMV) is a major cause of morbidity and mortality in transplant patients and in fetuses following congenital infection. The glycoprotein complexes gH/gL/gO and gH/gL/UL128/UL130/UL131A (Pentamer) are required for HCMV entry in fibroblasts and endothelial/epithelial cells, respectively, and are targeted by potently neutralizing antibodies in the infected host. Using purified soluble forms of gH/gL/gO and Pentamer as well as a panel of naturally elicited human monoclonal antibodies, we determined the location of key neutralizing epitopes on the gH/gL/gO and Pentamer surfaces. Mass Spectrometry (MS) coupled to Chemical Crosslinking or to Hydrogen Deuterium Exchange was used to define residues that are either in proximity or part of neutralizing epitopes on the glycoprotein complexes. We also determined the molecular architecture of the gH/gL/gO- and Pentamer-antibody complexes by Electron Microscopy (EM) and 3D reconstructions. The EM analysis revealed that the Pentamer specific neutralizing antibodies bind to two opposite surfaces of the complex, suggesting that they may neutralize infection by different mechanisms. Together, our data identify the location of neutralizing antibodies binding sites on the gH/gL/gO and Pentamer complexes and provide a framework for the development of antibodies and vaccines against HCMV.
External linksPLoS Pathog / PubMed:26485028 / PubMed Central
MethodsEM (single particle)
Resolution18.0 - 30.0 Å
Structure data

EMDB-6431:
RCT reconstruction of CMV gHgLgO and pentameric complexes bound to highly neutralizing antibodies
Method: EM (single particle) / Resolution: 18.0 Å

EMDB-6432:
RCT reconstruction of glycoprotein gHgLgO in complex with neutralizing Fab fragments 3G16 and 13H11
Method: EM (single particle) / Resolution: 19.0 Å

EMDB-6436:
RCT reconstruction of CMV complex
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-6437:
RCT reconstruction of CMV protein complex
Method: EM (single particle) / Resolution: 30.0 Å

EMDB-6438:
Structure of CMV protein complex
Method: EM (single particle) / Resolution: 25.0 Å

Source
  • Cytomegalovirus
  • unidentified (others)

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