6vy5

From Proteopedia

Jump to: navigation, search

Crystal structure of Nipah receptor binding protein head domain in complex with human neutralizing antibody HENV-26

Structural highlights

6vy5 is a 3 chain structure with sequence from Henipavirus nipahense and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.4Å
Ligands:NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GLYCP_NIPAV Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.[1] [2]

Publication Abstract from PubMed

Hendra (HeV) and Nipah (NiV) viruses are emerging zoonotic pathogens in the Henipavirus genus causing outbreaks of disease with very high case fatality rates. Here, we report the first naturally occurring human monoclonal antibodies (mAbs) against HeV receptor binding protein (RBP). All isolated mAbs neutralized HeV, and some also neutralized NiV. Epitope binning experiments identified five major antigenic sites on HeV-RBP. Animal studies demonstrated that the most potent cross-reactive neutralizing mAbs, HENV-26 and HENV-32, protected ferrets in lethal models of infection with NiV Bangladesh 3 days after exposure. We solved the crystal structures of mAb HENV-26 in complex with both HeV-RBP and NiV-RBP and of mAb HENV-32 in complex with HeV-RBP. The studies reveal diverse sites of vulnerability on RBP recognized by potent human mAbs that inhibit virus by multiple mechanisms. These studies identify promising prophylactic antibodies and define protective epitopes that can be used in rational vaccine design.

Potent Henipavirus Neutralization by Antibodies Recognizing Diverse Sites on Hendra and Nipah Virus Receptor Binding Protein.,Dong J, Cross RW, Doyle MP, Kose N, Mousa JJ, Annand EJ, Borisevich V, Agans KN, Sutton R, Nargi R, Majedi M, Fenton KA, Reichard W, Bombardi RG, Geisbert TW, Crowe JE Jr Cell. 2020 Dec 10;183(6):1536-1550.e17. doi: 10.1016/j.cell.2020.11.023. PMID:33306954[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Loading citation details..
Citations
3 reviews cite this structure
Liew et al. (2022)
No citations found

See Also

References

  1. Diederich S, Maisner A. Molecular characteristics of the Nipah virus glycoproteins. Ann N Y Acad Sci. 2007 Apr;1102:39-50. PMID:17470910 doi:http://dx.doi.org/10.1196/annals.1408.003
  2. Diederich S, Moll M, Klenk HD, Maisner A. The nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem. 2005 Aug 19;280(33):29899-903. Epub 2005 Jun 16. PMID:15961384 doi:http://dx.doi.org/10.1074/jbc.M504598200
  3. Dong J, Cross RW, Doyle MP, Kose N, Mousa JJ, Annand EJ, Borisevich V, Agans KN, Sutton R, Nargi R, Majedi M, Fenton KA, Reichard W, Bombardi RG, Geisbert TW, Crowe JE Jr. Potent Henipavirus Neutralization by Antibodies Recognizing Diverse Sites on Hendra and Nipah Virus Receptor Binding Protein. Cell. 2020 Dec 10;183(6):1536-1550.e17. PMID:33306954 doi:10.1016/j.cell.2020.11.023

Contents


PDB ID 6vy5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools