Characterization of a Phosphoprotein Associated with the SS-B/La Nuclear Antigen in Adenovirus-infected and Uninfected KB Cells

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1983 Jul 1

PMID 6193414

Citations 16

Authors

L I PIZER

J S Deng

R M Stenberg

E M Tan

Affiliations

Soon will be listed here.

Abstract

We have employed sera from patients with autoimmune disease to characterize the nuclear SS-B/La antigen in uninfected and adenovirus-infected KB cells. A 45,000-dalton phosphorylated polypeptide was specifically precipitated with anti-SS-B sera, and the level of phosphorylation was increased after infection. The increased phosphorylation appears to occur at the same amino acid residues phosphorylated in uninfected cells and results from increased phosphorylating activity rather than from altered enzyme specificity. A competition experiment between infected and uninfected cell extracts indicates that the antigen in the infected cell binds more strongly to SS-B/La antibodies. Fragments of adenovirus-induced virus-associated RNA as well as intact molecules complex with SS-B/La antigen and are immune precipitated with autoimmune sera.

Citing Articles

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Preferential recognition of the phosphorylated major linear B-cell epitope of La/SSB 349-368 aa by anti-La/SSB autoantibodies from patients with systemic autoimmune diseases.

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Phosphorylation of the Saccharomyces cerevisiae La protein does not appear to be required for its functions in tRNA maturation and nascent RNA stabilization.

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La autoantigen specifically recognizes a predicted stem-loop in hepatitis B virus RNA.

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Mosquito homolog of the La autoantigen binds to Sindbis virus RNA.

Pardigon N, Strauss J J Virol. 1996; 70(2):1173-81.

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