Download Reoviruses: Entry, Assembly and Morphogenesis (Current by Polly Roy PDF

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By Polly Roy

A evaluation of our present figuring out of Reoviridae access, disassembly/assembly and egress as well as updating excessive solution buildings of virus proteins and capsids from 3 diverse genera of the relations. such a lot of our preliminary realizing of molecular biology and procedures interested in virus replication and pathogenesis for the family members used to be generated from reovirus experiences. This ebook will curiosity researchers and scientists within the box of virology.

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Additional resources for Reoviruses: Entry, Assembly and Morphogenesis (Current Topics in Microbiology and Immunology)

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Figure and legend modified from Ebert et al. [50]) polymorphisms in the C-terminus determine susceptibility to proteolysis, the initial cleavage of σ3 probably occurs in this region. During proteolysis by cathepsin L, subsequent cleavages occur between residues 243–244 and 250–251 [50] (Fig. 7A). These cleavage sites are physically located near the Cterminus in the σ3 crystal structure [112] (Fig. 7C). Because of this proximity, the small end fragment released following initial cathepsin L cleavage likely exposes the other two sites, rendering them sensitive to subsequent cleavage Attachment and Cell Entry of Mammalian Orthoreovirus 21 events.

12. 13. 14. 15. 16. 17. 18. 19. 20. 21. 22. 29 Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, Hanada K (1982) L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J 201:189–198 Barton ES, Connolly JL, Forrest JC, Chappell JD, Dermody TS (2001) Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200–2211 Barton ES, Forrest JC, Connolly JL, Chappell JD, Liu Y, Schnell F, Nusrat A, Parkos CA, Dermody TS (2001) Junction adhesion molecule is a receptor for reovirus.

Concordantly, cathepsin L mediates reovirus disassembly more efficiently than cathepsin B in vitro [50]. These results demonstrate that either cathepsin L or cathepsin B is required for reovirus entry into murine fibroblasts and indicate that cathepsin L is the primary mediator of reovirus disassembly in these cells. Proteases other than cathepsin B and cathepsin L also are capable of ISVP formation. In P388D cells, a macrophage-like cell line, cathepsin S mediates uncoating of some strains of reovirus [68].

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