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Mutations in OAS1 genes

Inactive Publication Date: 2006-12-07
KINETA TWO LLC
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  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0054] The invention still further relates to a method of preventing infection by a flavivirus in a human subject susceptible to the infection, comprising administering to the human subject an OAS1 inhibitor selected from group consisting of an antisense oligonucleotide, a ribozyme, an RNAi, a protein, a polypeptide, an antibody, and a small molecule, wherein said OAS1 inhibitor prevents infection by said flavivirus.

Problems solved by technology

2-SAs bind to and activate RNase I, which degrades viral and cellular RNAs, leading to inhibition of cellular protein synthesis and impairment of viral replication.

Method used

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  • Mutations in OAS1 genes

Examples

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example 1

Amino Acid Modifications in Non-human Primate OAS1 Proteins

[0201] OAS1 genes from non-human primates were sequenced and compared with mutations found in the human OAS1 gene. Such mutations provide additional insight into evolution of the OAS1 gene and protein. Evolutionarily conserved amino acids suggest sites important, or critical, for OAS1 function or enzymatic activity. Conversely, OAS1 amino acid sites that have recently mutated, for example in humans only, or show a plurality of amino acid substitutions across primates, indicate sites less critical to function or enzymatic activity. The abundance of mutated sites within a particular motif of the OAS1 protein are correlated with the tolerance of that functional domain to modification. Such sites and motifs are optimized to improve protein function or specific activity. Similarly, mutations in genes and proteins with immune or viral defense functions like OAS1 are hypothesized to result from historical challenge by viral infect...

example 2

Preparation and Sequencing of cDNA

[0204] Total cellular RNA is purified from cultured lymphoblasts or fibroblasts from the patients having the hepatitis C resistance phenotype. The purification procedure is performed as described by Chomczynski, et al., Anal. Biochem., 162:156-159 (1987). The cells are homogenized in 10 milliliters (ml) of a denaturing solution containing 4.0M guanidine thiocyanate, 0.1M Tris-HCl at pH 7.5, and 0.1M beta-mercaptoethanol to form a cell lysate. Sodium lauryl sarcosinate is then admixed to a final concentration of 0.5% to the cell lysate after which the admixture was centrifuged at 5000×g for 10 minutes at room temperature. The resultant supernatant containing the total RNA is layered onto a cushion of 5.7M cesium chloride and 0.01M EDTA at pH 7.5 and is pelleted by centrifugation. The resultant RNA pellet is dissolved in a solution of 10 mM Tris-HCl at pH 7.6 and 1 mM EDTA (TE) containing 0.1% sodium docecyl sulfate (SDS). After phenolchloroform extr...

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Abstract

Modified amino acid sequences of OAS1 proteins in non-human primates, and genes related thereto, are provided.

Description

RELATED APPLICATIONS [0001] The present application claims benefit of priority from U.S. Provisional Patent Application titled MUTATIONS IN OAS1 GENES Ser. No. 60 / 677,680 filed May 4, 2005, under 35 U.S.C. §119. The foregoing provisional patent application is incorporated herein by reference in its entirety.TECHNICAL FIELD [0002] The present invention relates to a method for detecting a mutation in a human or non-human primate oligoadenylate synthetase gene, and to OAS1 proteins having at least one amino acid modification. BACKGROUND OF THE INVENTION [0003] A number of diseases have been identified to date in which natural resistance to infection exists in the human population. Alter and Moyer, J. Acquir. Immune Defic. Syndr. Hum Retrovirol. 18 Suppl. 1:S6-10 (1998) report hepatitis C viral infection (HCV) rates as high as 90% in high-risk groups such as injecting drug users. However, the mechanism by which the remaining 10% are apparently resistant to infection has not been identif...

Claims

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Application Information

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IPC IPC(8): C12Q1/68C07H21/04C12P21/06C12N9/22
CPCC12N9/1077C12N9/1241C12Q2600/156C12Q1/6883C12N9/88A61K38/00A61P31/04A61P31/12A61P31/14A61P31/16A61P31/18A61P31/20A61P31/22A61P35/00Y02A50/30C07K14/00C12N15/09
Inventor IADONATO, SHAWNMAGNESS, CHARLESFELLIN, P.SCHERER, CHRISTINAHAGEN, TORYOLSON, AMY
Owner KINETA TWO LLC
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