5NOP

Structure of Mojiang virus attachment glycoprotein

Summary for 5NOP

• Entry DOI: 10.2210/pdb5nop/pdb
• Descriptor: Attachment glycoprotein, CHLORIDE ION (3 entities in total)
• Functional Keywords: paramyxovirus, henipavirus, viral attachment, virus entry, 6-bladed beta-propeller, viral protein
• Biological source: Mojiang virus
• Total number of polymer chains: 2
• Total formula weight: 104902.30

Authors

Rissanen, I.R.,Ahmed, A.A.,Beaty, S.,Azarm, K.,Hong, P.,Nambulli, S.,Duprex, P.W.,Lee, B.,Bowden, T.A. (deposition date: 2017-04-12, release date: 2017-07-19, Last modification date: 2024-11-13)

Primary citation

Rissanen, I.,Ahmed, A.A.,Azarm, K.,Beaty, S.,Hong, P.,Nambulli, S.,Duprex, W.P.,Lee, B.,Bowden, T.A.
Idiosyncratic Mojiang virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses.
Nat Commun, 8:16060-16060, 2017

PubMed Abstract: In 2012, cases of lethal pneumonia among Chinese miners prompted the isolation of a rat-borne henipavirus (HNV), Mòjiāng virus (MojV). Although MojV is genetically related to highly pathogenic bat-borne henipaviruses, the absence of a conserved ephrin receptor-binding motif in the MojV attachment glycoprotein (MojV-G) indicates a differing host-cell recognition mechanism. Here we find that MojV-G displays a six-bladed β-propeller fold bearing limited similarity to known paramyxoviral attachment glycoproteins, in particular at host receptor-binding surfaces. We confirm the inability of MojV-G to interact with known paramyxoviral receptors in vitro, indicating an independence from well-characterized ephrinB2/B3, sialic acid and CD150-mediated entry pathways. Furthermore, we find that MojV-G is antigenically distinct, indicating that MojV would less likely be detected in existing large-scale serological screening studies focused on well-established HNVs. Altogether, these data indicate a unique host-cell entry pathway for this emerging and potentially pathogenic HNV.

PubMed: 28699636
DOI: 10.1038/ncomms16060

Experimental method

X-RAY DIFFRACTION (1.94 Å)