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Characteristics of Human OAS1 Isoform Proteins

by 1,†, 1,2,† and 1,*
Department of Biology, Georgia State University, Atlanta, GA 30303, USA
Research Center for Emerging Infections and Zoonosis (RIZ), University of Veterinary Medicine Hannover, 30559 Hannover, Germany
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Viruses 2020, 12(2), 152;
Received: 1 November 2019 / Revised: 20 January 2020 / Accepted: 22 January 2020 / Published: 29 January 2020
(This article belongs to the Special Issue Viruses and the OAS-RNase L Pathway)
The human OAS1 (hOAS1) gene produces multiple possible isoforms due to alternative splicing events and sequence variation among individuals, some of which affect splicing. The unique C-terminal sequences of the hOAS1 isoforms could differentially affect synthetase activity, protein stability, protein partner interactions and/or cellular localization. Recombinant p41, p42, p44, p46, p48, p49 and p52 hOAS1 isoform proteins expressed in bacteria were each able to synthesize trimer and higher order 2′-5′ linked oligoadenylates in vitro in response to poly(I:C). The p42, p44, p46, p48 and p52 isoform proteins were each able to induce RNase-mediated rRNA cleavage in response to poly(I:C) when overexpressed in HEK293 cells. The expressed levels of the p42 and p46 isoform proteins were higher than those of the other isoforms, suggesting increased stability in mammalian cells. In a yeast two-hybrid screen, Fibrillin1 (FBN1) was identified as a binding partner for hOAS1 p42 isoform, and Supervillin (SVIL) as a binding partner for the p44 isoform. The p44-SVIL interaction was supported by co-immunoprecipitation data from mammalian cells. The data suggest that the unique C-terminal regions of hOAS1 isoforms may mediate the recruitment of different partners, alternative functional capacities and/or different cellular localization. View Full-Text
Keywords: human OAS1 isoforms; 2-5A; rRNA cleavage; Fibrillin1; supervillin human OAS1 isoforms; 2-5A; rRNA cleavage; Fibrillin1; supervillin
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MDPI and ACS Style

Di, H.; Elbahesh, H.; Brinton, M.A. Characteristics of Human OAS1 Isoform Proteins. Viruses 2020, 12, 152.

AMA Style

Di H, Elbahesh H, Brinton MA. Characteristics of Human OAS1 Isoform Proteins. Viruses. 2020; 12(2):152.

Chicago/Turabian Style

Di, Han; Elbahesh, Husni; Brinton, Margo A. 2020. "Characteristics of Human OAS1 Isoform Proteins" Viruses 12, no. 2: 152.

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