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TitleNon-overlapping epitopes on the gHgL-gp42 complex for the rational design of a triple-antibody cocktail against EBV infection.
Journal, issue, pagesCell Rep Med, Vol. 4, Issue 11, Page 101296, Year 2023
Publish dateNov 21, 2023
AuthorsJunping Hong / Ling Zhong / Liqin Liu / Qian Wu / Wanlin Zhang / Kaiyun Chen / Dongmei Wei / Hui Sun / Xiang Zhou / Xinyu Zhang / Yin-Feng Kang / Yang Huang / Junyu Chen / Guosong Wang / Yan Zhou / Yanhong Chen / Qi-Sheng Feng / Hai Yu / Shaowei Li / Mu-Sheng Zeng / Yi-Xin Zeng / Miao Xu / Qingbing Zheng / Yixin Chen / Xiao Zhang / Ningshao Xia /
PubMed AbstractEpstein-Barr virus (EBV) is closely associated with cancer, multiple sclerosis, and post-acute coronavirus disease 2019 (COVID-19) sequelae. There are currently no approved therapeutics or vaccines ...Epstein-Barr virus (EBV) is closely associated with cancer, multiple sclerosis, and post-acute coronavirus disease 2019 (COVID-19) sequelae. There are currently no approved therapeutics or vaccines against EBV. It is noteworthy that combining multiple EBV glycoproteins can elicit potent neutralizing antibodies (nAbs) against viral infection, suggesting possible synergistic effects. Here, we characterize three nAbs (anti-gp42 5E3, anti-gHgL 6H2, and anti-gHgL 10E4) targeting different glycoproteins of the gHgL-gp42 complex. Two antibody cocktails synergistically neutralize infection in B cells (5E3+6H2+10E4) and epithelial cells (6H2+10E4) in vitro. Moreover, 5E3 alone and the 5E3+6H2+10E4 cocktail confer potent in vivo protection against lethal EBV challenge in humanized mice. The cryo-EM structure of a heptatomic gHgL-gp42 immune complex reveals non-overlapping epitopes of 5E3, 6H2, and 10E4 on the gHgL-gp42 complex. Structural and functional analyses highlight different neutralization mechanisms for each of the three nAbs. In summary, our results provide insight for the rational design of therapeutics or vaccines against EBV infection.
External linksCell Rep Med / PubMed:37992686 / PubMed Central
MethodsEM (single particle)
Resolution3.52 - 3.64 Å
Structure data

33990

7yoy

EMDB-33990, PDB-7yoy:
Cryo-EM structure of EBV gHgL-gp42 in complex with mAbs 3E8 and 5E3 (localized refinement)
Method: EM (single particle) / Resolution: 3.64 Å

33992

7yp1

EMDB-33992, PDB-7yp1:
Cryo-EM structure of EBV gHgL-gp42 in complex with mAb 10E4 (localized refinement)
Method: EM (single particle) / Resolution: 3.54 Å

EMDB-33993: Cryo-EM density map of EBV gHgL-gp42 in complex with four mAbs 5E3, 3E8, 6H2 and 10E4
Method: EM (single particle) / Resolution: 3.59 Å

33994

7yp2

EMDB-33994, PDB-7yp2:
Cryo-EM structure of EBV gHgL-gp42 in complex with mAb 6H2 (localized refinement)
Method: EM (single particle) / Resolution: 3.52 Å

Source
  • human gammaherpesvirus 4 (Epstein-Barr virus)
  • oryctolagus cuniculus (rabbit)
  • mus musculus (house mouse)
KeywordsVIRAL PROTEIN / EBV / Cryo-EM / Glycoprotein / gHgL-gp42 complex / Antibody

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