Reoviruses I: Structure, Proteins, and Genetics
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Outer capsid protein mu-1
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B , intensities of bands corresponding to reovirus proteins were quantified using the Odyssey software package LI-COR. Infectivity of reovirus variants. The titer of each preparation was determined by plaque assay. Data points indicate independent viral purifications. To assess whether the differences in protease sensitivity of our variant viruses correlate with biochemical measures of capsid stability, we determined the relative loss of titer of our variant panel following heat treatment.
M2 - Outer capsid protein mu-1 - Reovirus type 1 (strain Lang) (T1L) - M2 gene & protein
Aliquots were removed at min intervals, and titers were determined by plaque assay Fig. The rate of titer loss for that virus did not significantly differ from T3D. The fact that enhanced protease sensitivity and altered sensitivity to heat are correlated in the context of YH suggests that this residue controls both properties through a common structural mechanism.
Resistance of reovirus variants to inactivation by heat. At min intervals, samples were removed and placed on ice for 15 min.
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Titers were determined by plaque assay. Results are presented as the percentage of mean viral titer of untreated samples per interval of incubation, for triplicate experiments. Following binding to cell-surface receptors, reovirus particles are thought to be internalized via clathrin-dependent endocytosis 10 , — , 12 , Cells were incubated overnight and scored for viral infectivity by indirect immunofluorescence Fig. These findings indicate that enhanced outer capsid protease sensitivity accelerates access of reovirus to the cytoplasm for subsequent steps in its replication cycle.
Kinetics of ammonium chloride bypass by reovirus variants. Monolayers of L cells were adsorbed with reovirus variants at an m. At the times shown after adsorption, ammonium chloride was added to a final concentration of 25 m m.
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The results are presented as the percentage of cells infected, normalized to untreated wells, for triplicate experiments. To determine whether these second-site mutations affect reovirus disassembly, we tested the effect of E64 treatment on the replication of variants containing these alterations Fig. E64 sensitivity of reovirus strains with second-site mutations.
The medium was removed, and cells were adsorbed with reovirus strains at an m. Nonenveloped viruses must undergo particle disassembly to initiate an infectious cycle. However, this model has not been explicitly tested. The importance of capsid stability in other phases of the reovirus life cycle is unclear.
To our knowledge, reovirus strain T3A is the only field isolate strain reported to date that contains a histidine at position We also observed that T3A and T3D have similar in vitro disassembly kinetics when treated with the endosomal protease cathepsin L. We used plasmid-based reverse genetics to generate a panel of reovirus variants to test the contributions made by each T3A-T3D polymorphic residue to capsid stability in an otherwise isogenic background that includes YH. The recovered variant viruses had no overt defects in replication or specific infectivity Fig. Together, these results provide strong evidence that suppression of the YH phenotype in T3A is solely attributable to the glycine-to-glutamate polymorphism at position The observation that residue suppresses YH indirectly supports this model Fig.
This increase in density may represent the dislocated C terminus of the molecule. It is possible that the glycine-to-glutamate polymorphism observed in T3A stabilizes the C terminus through charge-charge interactions with His In that study, Arg failed to suppress YH, perhaps because it fails to neutralize the basic charge of His The C terminus is depicted in red.
Glu and His are modeled in yellow and green , respectively, and are drawn in stick representation. The amino acids corresponding to the two putative cathepsin L cleavage sites, residues ValThr and GlyHis 16 , are shown in black in stick representation. The reovirus life cycle involves fecal-oral transmission between infected hosts, a step that requires some degree of resistance to degradation. Viruses with diminished outer capsid stability may have decreased viability outside a mammalian host, which would reduce their likelihood of encountering a new host.
However, it is possible that destabilization of the outer capsid adversely affects other aspects of viral replication or virus-host interactions. The optimum stability of reovirus capsid structures may also depend on the specific proteolytic milieu of the various physiological compartments encountered by viral particles during the course of infection. More work is necessary to define the precise constraints on reovirus capsid stability throughout the viral life cycle.
We express our appreciation to Karl Boehme and Greg Wilson for careful review of the manuscript and to Chris Aiken for helpful suggestions. We thank John Mort for the kind gift of purified cathepsin L. This work was also supported by the Elizabeth B. Lamb Center for Pediatric Research. You'll be in good company. Journal of Lipid Research.
Previous Section Next Section. Specific Infectivity of Reovirus Virions Fresh preparations of reovirus virions were generated in triplicate from second-passage lysate stocks as described View this table: In this window In a new window. Outer Capsid Mutations Affect Reovirus Heat Sensitivity To assess whether the differences in protease sensitivity of our variant viruses correlate with biochemical measures of capsid stability, we determined the relative loss of titer of our variant panel following heat treatment.
Enhanced Outer Capsid Protease Sensitivity Facilitates Endosomal Escape Following binding to cell-surface receptors, reovirus particles are thought to be internalized via clathrin-dependent endocytosis 10 , — , 12 , Previous Section. Wilson I.
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