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TitleA nanobody specific to prefusion glycoprotein B neutralizes HSV-1 and HSV-2.
Journal, issue, pagesNature, Vol. 646, Issue 8084, Page 433-441, Year 2025
Publish dateSep 3, 2025
AuthorsBenjamin Vollmer / Henriette Ebel / Renate Rees / Julia Nentwig / Thomas Mulvaney / Jürgen Schünemann / Jens Krull / Maya Topf / Dirk Görlich / Kay Grünewald /
PubMed AbstractThe nine human herpesviruses, including herpes simplex virus 1 and 2, human cytomegalovirus and Epstein-Barr virus, present a significant burden to global public health. Their envelopes contain at ...The nine human herpesviruses, including herpes simplex virus 1 and 2, human cytomegalovirus and Epstein-Barr virus, present a significant burden to global public health. Their envelopes contain at least ten different glycoproteins, which are necessary for host cell tropism, attachment and entry. The best conserved among them, glycoprotein B (gB), is essential as it performs membrane fusion by undergoing extensive rearrangements from a prefusion to postfusion conformation. At present, there are no antiviral drugs targeting gB or neutralizing antibodies directed against its prefusion form, because of the difficulty in structurally determining and using this metastable conformation. Here we show the isolation of prefusion-specific nanobodies, one of which exhibits strong neutralizing and cross-species activity. By mutational stabilization we solved the herpes simplex virus 1 gB full-length prefusion structure, which allowed the bound epitope to be determined. Our analyses show the membrane-embedded regions of gB and previously unresolved structural features, including a new fusion loop arrangement, providing insights into the initial conformational changes required for membrane fusion. Binding an epitope spanning three domains, proximal only in the prefusion state, the nanobody keeps wild-type HSV-2 gB in this conformation and enabled its native prefusion structure to be determined. This also indicates the mode of neutralization and an attractive avenue for antiviral interventions.
External linksNature / PubMed:40903574 / PubMed Central
MethodsEM (single particle)
Resolution2.21 - 3.0 Å
Structure data

52863

9ih8

EMDB-52863, PDB-9ih8:
HSV-2 postfusion glycoprotein B
Method: EM (single particle) / Resolution: 2.21 Å

52963

9ih8

9q9l

EMDB-52963, PDB-9q9l:
HSV-1 prefusion glycoprotein B
PDB-9ih8: HSV-2 postfusion glycoprotein B
Method: EM (single particle) / Resolution: 2.64 Å

52965

9ih8

9q9n

EMDB-52965, PDB-9q9n:
HSV-1 prefusion glycoprotein B bound by Nb1_gbHSV
PDB-9ih8: HSV-2 postfusion glycoprotein B
Method: EM (single particle) / Resolution: 3.0 Å

52966

9ih8

9q9s

EMDB-52966, PDB-9q9s:
HSV-2 prefusion glycoprotein B bound by Nb1_gbHSV
PDB-9ih8: HSV-2 postfusion glycoprotein B
Method: EM (single particle) / Resolution: 2.7 Å

Source
  • human herpesvirus 2 strain 333
  • human alphaherpesvirus 1 strain 17
  • vicugna pacos (alpaca)
KeywordsVIRAL PROTEIN / Glycoprotein B / viral membrane fusion protein / Herpes simplex virus 2 / HSV-2 / gB / Herpes simplex virus 1 / HSV-1 / nanobody / nanobody complex

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