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TitleStructural basis for the shared neutralization mechanism of three classes of human papillomavirus type 58 antibodies with disparate modes of binding.
Journal, issue, pagesJ Virol, Vol. 95, Issue 7, Year 2021
Publish dateJan 20, 2021
AuthorsMaozhou He / Xin Chi / Zhenghui Zha / Yunbing Li / Jie Chen / Yang Huang / Shiwen Huang / Miao Yu / Zhiping Wang / Shuo Song / Xinlin Liu / Shuangping Wei / Zekai Li / Tingting Li / Yingbin Wang / Hai Yu / Qinjian Zhao / Jun Zhang / Qingbing Zheng / Ying Gu / Shaowei Li / Ningshao Xia /
PubMed AbstractHuman papillomavirus type 58 (HPV58) is associated with cervical cancer and poses a significant health burden worldwide. Although the commercial 9-valent HPV vaccine covers HPV58, the structural and ...Human papillomavirus type 58 (HPV58) is associated with cervical cancer and poses a significant health burden worldwide. Although the commercial 9-valent HPV vaccine covers HPV58, the structural and molecular-level neutralization sites of the HPV58 complete virion are not fully understood. Here, we report the high-resolution (∼3.5 Å) structure of the complete HPV58 pseudovirus (PsV58) using cryo-electron microscopy (cryo-EM). Three representative neutralizing monoclonal antibodies (nAbs 5G9, 2H3 and A4B4) were selected through clustering from a nAb panel against HPV58. Bypassing the steric hindrance and symmetry-mismatch in the HPV Fab-capsid immune-complex, we present three different neutralizing epitopes in the PsV58, and show that, despite differences in binding, these nAbs share a common neutralization mechanism. These results offer insight into HPV58 genotype specificity and broaden our understanding of HPV58 neutralization sites for antiviral research. Cervical cancer primarily results from persistent infection with high-risk types of human papillomavirus (HPV). HPV type 58 (HPV58) is an important causative agent, especially within Asia. Despite this, we still have limited data pertaining to the structural and neutralizing epitopes of HPV58, and this encumbers our in-depth understanding of the virus mode of infection. Here, we show that representative nAbs (5G9, 10B11, 2H3, 5H2 and A4B4) from three different groups share a common neutralization mechanism that appears to prohibit the virus from associating with the extracellular matrix and cell surface. Furthermore, we identify that the nAbs engage via three different binding patterns: top-center binding (5G9 and 10B11), top-fringe binding (2H3 and 5H2), and fringe binding (A4B4). Our work shows that, despite differences in the pattern in binding, nAbs against HPV58 share a common neutralization mechanism. These results provide new insight into the understanding of HPV58 infection.
External linksJ Virol / PubMed:33472937 / PubMed Central
MethodsEM (single particle)
Resolution3.5 - 6.43 Å
Structure data

EMDB-30768:
2-fold subparticles refinement of human papillomavirus type 58 pseudovirus
Method: EM (single particle) / Resolution: 3.63 Å

EMDB-30769:
3-fold sub-particles refinement of human papillomavirus type 58 pseudovirus
Method: EM (single particle) / Resolution: 3.66 Å

EMDB-30770:
5-fold sub-particles refinement of human papillomavirus type 58 pseudovirus
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-30772:
The cryo-EM structure of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 5G9
Method: EM (single particle) / Resolution: 4.67 Å

EMDB-30773:
The cryo-EM structure of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 10B11
Method: EM (single particle) / Resolution: 6.43 Å

EMDB-30774:
The cryo-EM structure of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 2H3
Method: EM (single particle) / Resolution: 4.08 Å

EMDB-30777:
The cryo-EM structure of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 5H2
Method: EM (single particle) / Resolution: 4.33 Å

EMDB-30780:
The cryo-EM structure of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of A4B4
Method: EM (single particle) / Resolution: 4.23 Å

30781

7dn5

EMDB-30781, PDB-7dn5:
The cryo-EM structure of human papillomavirus type 58 pseudovirus
Method: EM (single particle) / Resolution: 4.11 Å

30783

7dnh

EMDB-30783, PDB-7dnh:
2-fold subparticles refinement of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 2H3
Method: EM (single particle) / Resolution: 3.64 Å

30786

7dnk

EMDB-30786, PDB-7dnk:
2-fold subparticles refinement of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of 5G9
Method: EM (single particle) / Resolution: 6.41 Å

30787

7dnl

EMDB-30787, PDB-7dnl:
2-fold subparticles refinement of human papillomavirus type 58 pseudovirus in complexed with the Fab fragment of A4B4
Method: EM (single particle) / Resolution: 4.19 Å

Source
  • human papillomavirus type 58
  • mus musculus (house mouse)
KeywordsVIRUS / particles / VIRAL PROTEIN/IMMUNE SYSTEM / Immune complex / VIRAL PROTEIN-IMMUNE SYSTEM complex / IMMUNE SYSTEM/VIRAL PROTEIN / VIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN complex

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