Anatomy and evolution of proteins displaying the viral capsid jellyroll topology

Chelvanayagam, Gareth; Heringa, Jaap; Argos, Patrick

doi:10.1016/0022-2836(92)90502-b

Cited by 60 publications

(28 citation statements)

References 58 publications

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“…Structural studies of the coat protein subunit of tomato bushy stunt virus, a close relative of CNV, have shown that the shell domain folds into a jellyroll-type structure typical of several plant and animal virus coat protein subunits (6). Interestingly, the lectin ConA also folds into a jellyroll-type structure (6).…”

Section: Discussionmentioning

confidence: 99%

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Evidence that Binding of Cucumber Necrosis Virus to Vector Zoospores Involves Recognition of Oligosaccharides

Kakani

Robbins

Rochon

2003

J Virol

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Section: Discussionmentioning

confidence: 99%

“…Interestingly, the lectin ConA also folds into a jellyroll-type structure (6). Indeed, it has been suggested (2) that the overall similarity in structural topology between the tombusvirus capsid and ConA may indicate that tombusviruses have evolved from lectins.…”

Section: Discussionmentioning

confidence: 99%

Evidence that Binding of Cucumber Necrosis Virus to Vector Zoospores Involves Recognition of Oligosaccharides

Kakani

Robbins

Rochon

2003

J Virol

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“…The model has exceptional geometry, with 93% of the residues in the most favored regions of the Ramachandran plot (see Table 1). Strands in the jellyroll motif were labeled according to convention (29). The GdnHCltreated knob was crystallized under the same conditions as the wild type knob.…”

Section: Methodsmentioning

confidence: 99%

Atomic Structure of Bacteriophage Sf6 Tail Needle Knob

Bhardwaj

Molineux

Casjens

et al. 2011

Journal of Biological Chemistry

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Podoviridae are double-stranded DNA bacteriophages that use short, non-contractile tails to adsorb to the host cell surface. Within the tail apparatus of P22-like phages, a dedicated fiber known as the "tail needle" likely functions as a cell envelopepenetrating device to promote ejection of viral DNA inside the host. In Sf6, a P22-like phage that infects Shigella flexneri, the tail needle presents a C-terminal globular knob. This knob, absent in phage P22 but shared in other members of the P22-like genus, represents the outermost exposed tip of the virion that contacts the host cell surface. Here, we report a crystal structure of the Sf6 tail needle knob determined at 1.0 Å resolution. The structure reveals a trimeric globular domain of the TNF fold structurally superimposable with that of the tail-less phage PRD1 spike protein P5 and the adenovirus knob, domains that in both viruses function in receptor binding. However, P22-like phages are not known to utilize a protein receptor and are thought to directly penetrate the host surface. At 1.0 Å resolution, we identified three equivalents of L-glutamic acid (L-Glu) bound to each subunit interface. Although intimately bound to the protein, L-Glu does not increase the structural stability of the trimer nor it affects its ability to self-trimerize in vitro. In analogy to P22 gp26, we suggest the tail needle of phage Sf6 is ejected through the bacterial cell envelope during infection and its C-terminal knob is threaded through peptidoglycan pores formed by glycan strands.

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“…6. The folding of the large capsid proteins of other tetraviruses involves eight β-sheets that assemble into the jelly roll structure associated with icosahedral virus capsids (Chelvanayagam et al, 1992). Eight regions of β-sheets were identified in TaV that align (Fig.…”

Section: Determining the Relationship Of Tav To Other Members Of The mentioning

confidence: 99%

A novel capsid expression strategy for Thosea asigna virus (Tetraviridae).

Pringle

Gordon

Hanzlik

et al. 1999

Journal of General Virology

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This paper presents evidence thatThe sequences indicate that the pre-protein is cleaved at two positions to produce the 56 and 6 kDa capsid proteins as well as a predicted third protein that was not detected in the mature virion. Phylogenetic analysis of the capsid proteins indicated that TaV is more closely related to NβV than to the Nudaurelia ω-like viruses. The eight β-sheets that make up a jelly roll structure in the TaV capsid protein were identified by computer analysis.

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Anatomy and evolution of proteins displaying the viral capsid jellyroll topology

Cited by 60 publications

References 58 publications

Evidence that Binding of Cucumber Necrosis Virus to Vector Zoospores Involves Recognition of Oligosaccharides

Evidence that Binding of Cucumber Necrosis Virus to Vector Zoospores Involves Recognition of Oligosaccharides

Atomic Structure of Bacteriophage Sf6 Tail Needle Knob

A novel capsid expression strategy for Thosea asigna virus (Tetraviridae).

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