VSV G CR2VSV G CR2

Structural highlights

5oyl is a 2 chain structure with sequence from Homo sapiens and Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B7UCZ5_9RHAB

Publication Abstract from PubMed

Vesicular stomatitis virus (VSV) is an oncolytic rhabdovirus and its glycoprotein G is widely used to pseudotype other viruses for gene therapy. Low-density lipoprotein receptor (LDL-R) serves as a major entry receptor for VSV. Here we report two crystal structures of VSV G in complex with two distinct cysteine-rich domains (CR2 and CR3) of LDL-R, showing that their binding sites on G are identical. We identify two basic residues on G, which are essential for its interaction with CR2 and CR3. Mutating these residues abolishes VSV infectivity even though VSV can use alternative receptors, indicating that all VSV receptors are members of the LDL-R family. Collectively, our data suggest that VSV G has specifically evolved to interact with receptor CR domains. These structural insights into the interaction between VSV G and host cell receptors provide a basis for the design of recombinant viruses with an altered tropism.

Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein.,Nikolic J, Belot L, Raux H, Legrand P, Gaudin Y, A Albertini A Nat Commun. 2018 Mar 12;9(1):1029. doi: 10.1038/s41467-018-03432-4. PMID:29531262[1]

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

See Also

References

  1. Nikolic J, Belot L, Raux H, Legrand P, Gaudin Y, A Albertini A. Structural basis for the recognition of LDL-receptor family members by VSV glycoprotein. Nat Commun. 2018 Mar 12;9(1):1029. doi: 10.1038/s41467-018-03432-4. PMID:29531262 doi:http://dx.doi.org/10.1038/s41467-018-03432-4

5oyl, resolution 2.25Å

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