By Moore R. L.
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Extra resources for An Extension of the Theorem That No Countable Point Set Is Perfect
L C is present in infectious subvirion particles of mammalian reoviruses and is proposed to have a role in penetration. J Virol 66:6408-6418 Nibert ML, Dermody TS, Fields BN (1990) Structure of the reovirus cell-attachment protein: a model for the domain organization of 0'1. J Virol 64:2976-2989 Nibert ML, Furlong DB. Fields BN (1991a) Mechanisms of viral pathogenesis. Distinct forms of reoviruses and their roles during replication in cells and host. J Clin Invest 88:727-734 Nibert ML, Schiff LA, Fields BN (1991b) Mammalian reoviruses contain a myristoylated struetural protein.
However, most, if not all, of the virion structural proteins also have enzymatic activities and/or other functions that are essential in the reovirus life cycle (Table 1). This structural pro tein pleiotropy is summarized in this chapter, which is based on the many studies that have correlated virion proteins with functional activities and assigned them to specific reovirus genome segments. 2 Entry of Reovirus into "ost Cells The entry phase of reovirus infection includes several distinct steps: attachment to the cell surface, endocytic uptake, internalization, and uncoating (NIBERT et al.
In the meantime, a fundamental question concerns what might be the structure of the retracted form. , conversion between ot-helix and ß-sheet structures), bending at hinges within the fiber, or deeper protrusion of the fiber into the ",2 channel? Another question concerns whether the retracted form of erl might make additional contacts with outer-capsid pro teins, particularly with er3 (VIRGIN et al. 1991), to explain the proposedswitch to the extended form in ISVPs. 3 Nature of the 0"1 Oligomer The strongest available data suggest that the reovirus T3D erl protein forms trimers (STRONG et al.
An Extension of the Theorem That No Countable Point Set Is Perfect by Moore R. L.