3BWR

SV40 VP1 pentamer in complex with GM1 oligosaccharide

Summary for 3BWR

• Entry DOI: 10.2210/pdb3bwr/pdb
• Related: 1SVA 3BWQ
• Descriptor: Capsid protein VP1, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose-(1-4)-[N-acetyl-alpha-neuraminic acid-(2-3)]beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: sv40, gm1, viral receptor, viral attachment, ganglioside, vp1, polyomaviruses, capsid protein, late protein, nucleus, virion, viral protein
• Biological source: Simian virus 40
• Cellular location: Virion: P03087
• Total number of polymer chains: 5
• Total formula weight: 152041.16

Authors

Neu, U.,Stehle, T. (deposition date: 2008-01-10, release date: 2008-03-04, Last modification date: 2024-11-13)

Primary citation

Neu, U.,Woellner, K.,Gauglitz, G.,Stehle, T.
Structural basis of GM1 ganglioside recognition by simian virus 40.
Proc.Natl.Acad.Sci.Usa, 105:5219-5224, 2008

PubMed Abstract: Simian virus 40 (SV40) has been a paradigm for understanding attachment and entry of nonenveloped viruses, viral DNA replication, and virus assembly, as well as for endocytosis pathways associated with caveolin and cholesterol. We find by glycan array screening that SV40 recognizes its ganglioside receptor GM1 with a quite narrow specificity, but isothermal titration calorimetry shows that individual binding sites have a relatively low affinity, with a millimolar dissociation constant. The high-resolution crystal structure of recombinantly produced SV40 capsid protein, VP1, in complex with the carbohydrate portion of GM1, reveals that the receptor is bound in a shallow solvent-exposed groove at the outer surface of the capsid. Through a complex network of interactions, VP1 recognizes a conformation of GM1 that is the dominant one in solution. Analysis of contacts provides a structural basis for the observed specificity and suggests binding mechanisms for additional physiologically relevant GM1 variants. Comparison with murine Polyomavirus (Polyoma) receptor complexes reveals that SV40 uses a different mechanism of sialic acid binding, which has implications for receptor binding of human polyomaviruses. The SV40-GM1 complex reveals a parallel to cholera toxin, which uses a similar cell entry pathway and binds GM1 in the same conformation.

PubMed: 18353982
DOI: 10.1073/pnas.0710301105

Experimental method

X-RAY DIFFRACTION (2.25 Å)