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The incorporation of reovirus cell attachment protein sigma 1 into virions requires the N-terminal hydrophobic tail and the adjacent heptad repeat region.

Abstract：

:The N-terminal portion of the reovirus cell attachment protein sigma 1 has recently been shown to possess intrinsic oligomerization and virion-anchoring functions. Sequence analysis of the sigma 1 proteins of the three reovirus serotypes has revealed the presence of distinct structural domains within this region: a terminal hydrophobic tail, a hinge, and an extended coiled-coil. To probe the inter-relationship between the virion-anchoring function and the oligomerization function, we constructed two serotype 3 (T3) sigma 1 deletion mutants in SV40 expression vectors, one lacking the hydrophobic tail and the hinge, and the other lacking an adjacent region which constituted part of the coiled-coil. These mutants were (i) expressed in uninfected COS-1 cells and assayed for their ability to form oligomers, and (ii) expressed in type 1 (T1) reovirus-infected COS-1 cells and assayed for their incorporability into progeny T1 virions. It was found that, whereas both truncated sigma 1 proteins were capable of forming stable oligomers, neither could be incorporated into virions. These observations, coupled with structural characteristics deduced from sequence analysis, are compatible with a model in which the hydrophobic tail is the bona fide sigma 1 anchorage domain and whose precise association with the virion spikes is dictated by an adjacent heptad repeat region linked to the former structure via a flexible hinge region.

journal_name

Virology

journal_title

Virology

authors

Leone G,Mah DC,Lee PW

doi

10.1016/0042-6822(91)90678-5

subject

Has Abstract

pub_date

1991-05-01 00:00:00

pages

346-50

issue

1

eissn

0042-6822

issn

1096-0341

pii

0042-6822(91)90678-5

journal_volume

182

pub_type

杂志文章

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