African swine fever virus protein A238L interacts with the cellular phosphatase calcineurin via a binding domain similar to that of NFAT.

Abstract:

:The African swine fever virus protein A238L inhibits activation of NFAT transcription factor by binding calcineurin and inhibiting its phosphatase activity. NFAT controls the expression of many immunomodulatory proteins. Here we describe a 14-amino-acid region of A238L that is needed and sufficient for binding to calcineurin. By introducing mutations within this region, we have identified a motif (PxIxITxC/S) required for A238L binding to calcineurin; a similar motif is found in NFAT proteins. Peptides corresponding to this domain of A238L bind calcineurin but do not inhibit its phosphatase activity. Binding of A238L to calcineurin stabilizes the A238L protein in cells. Although A238L-mediated suppression of NF-kappaB-dependent gene expression occurs by a different mechanism, the A238L-calcineurin interaction may be required to stabilize A238L.

journal_name

J Virol

journal_title

Journal of virology

authors

Miskin JE,Abrams CC,Dixon LK

doi

10.1128/jvi.74.20.9412-9420.2000

subject

Has Abstract

pub_date

2000-10-01 00:00:00

pages

9412-20

issue

20

eissn

0022-538X

issn

1098-5514

journal_volume

74

pub_type

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