The structure of simian virus 40 refined at 3.1 å resolution

Stehle, Thilo; Gamblin, S.J.; Yan, Yong-Bin; Harrison, Stephen C.

doi:10.1016/s0969-2126(96)00020-2

Cited by 287 publications

(438 citation statements)

References 67 publications

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“…Each VP1 assumes the established ␤-sandwich fold, with two four-stranded antiparallel ␤-sheets (containing ␤-strands C,H,E,F and B,I,D,G) forming the core structure. The ''unassembled'' VP1 structure solved here is very similar to that of the assembled VP1 protein in the structure of the SV40 capsid (5). The rmsd between the two proteins is 1.2 Å for the C␣ atoms of residues 45-297.…”

supporting

confidence: 52%

Structural basis of GM1 ganglioside recognition by simian virus 40

Neu

Woellner

Gauglitz

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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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.crystal structure ͉ glycan array ͉ polyomaviruses ͉ viral attachment ͉ protein-carbohydrate complex

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supporting

confidence: 52%

Structural basis of GM1 ganglioside recognition by simian virus 40

Neu

Woellner

Gauglitz

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

169

230

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“…These protrusions are morphologically similar to the C-terminal "arm-invading" model of polyomaviruses, which reinforce the invading arms via an interpentameric disulfide bridge(s) (Baker et al, 1989(Baker et al, , 1991Stehle et al, 1994Stehle et al, , 1996Sapp et al, 1998;Jao et al, 1999). While detailed information regarding the intra-and interpentameric molecular interactions between pentamers cannot be garnered from the current atomic structure of HPV16, assumptions can be made from this model.…”

Section: Structural Details Of Papillomavirus Particles High-resolutimentioning

confidence: 68%

Replication and Assembly of Human Papillomaviruses

Conway

Meyers²

2009

J Dent Res

119

101

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Human papillomaviruses (HPVs) are small dsDNA tumor viruses, which are the etiologic agents of most cervical cancers and are associated with a growing percentage of oropharyngeal cancers. The HPV capsid is non-enveloped, having a T=7 icosahedral symmetry formed via the interaction among 72 pentamers of the major capsid protein, L1. The minor capsid protein L2 associates with L1 pentamers, although it is not known if each L1 pentamer contains a single L2 protein. The HPV life cycle strictly adheres to the host cell differentiation program, and as such, native HPV virions are only produced in vivo or in organotypic "raft" culture. Research producing synthetic papillomavirus particles-such as virus-like particles (VLPs), papillomavirus-based gene transfer vectors, known as pseudovirions (PsV), and papillomavirus genome-containing quasivirions (QV)-has bypassed the need for stratifying and differentiating host tissue in viral assembly and has allowed for the rapid analysis of HPV infectivity pathways, transmission, immunogenicity, and viral structure.

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“…To stabilize the virus structure, each VP1 within a pentamer extends its carboxyterminal arm to an adjacent pentamer. Calcium ions bound to the virus further strengthen this interpentamer interaction (Stehle et al 1996). Finally, a network of VP1 disulfide bonds reinforces its overall architecture (Stehle et al 1996).…”

Section: Polyomavirus Co-opts the Er During Entrymentioning

confidence: 96%