The Many Faces of Oligoadenylate Synthetases

被引：7

作者：

Sarkar, Saumendra N. ^{[1
,2
,3
]}

Harioudh, Munesh K. ^{[1
,2
]}

Shao, Lulu ^{[1
,2
]}

Perez, Joseph ^{[1
,2
,4
]}

Ghosh, Arundhati ^{[1
,2
,5
]}

机构：

[1] Univ Pittsburgh, Sch Med, UPMC Hillman Canc Ctr, Canc Virol Program, Suite 1-8,5117 Ctr Ave, Pittsburgh, PA 15213 USA

[2] Univ Pittsburgh, Sch Med, Dept Microbiol & Mol Genet, Pittsburgh, PA USA

[3] Univ Pittsburgh, Sch Med, Dept Immunol, Pittsburgh, PA USA

[4] VectorBuilder Inc, Chicago, IL USA

[5] Nobel Life Sci Inc, Sykesville, MD USA

来源：

JOURNAL OF INTERFERON AND CYTOKINE RESEARCH | 2023年 / 43卷 / 11期

关键词：

interferon; oligoadenylate synthetase; West Nile virus; interferon-stimulated genes; antiviral mechanism; SPLICE-ACCEPTOR SITE; SINGLE-NUCLEOTIDE POLYMORPHISM; 2'; 5'-OLIGOADENYLATE SYNTHETASE; I INTERFERON; 2'-5'-OLIGOADENYLATE SYNTHETASE; PROTEIN-SYNTHESIS; RNASE-L; ANTIVIRAL ACTIVITY; OAS1; EXPRESSION;

D O I：

10.1089/jir.2023.0098

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

2 '-5 ' Oligoadenylate synthetases (OAS) are interferon-stimulated genes that are most well-known to protect hosts from viral infections. They are evolutionarily related to an ancient family of Nucleotidyltransferases, which are primarily involved in pathogen-sensing and innate immune response. Classical function of OAS proteins involves double-stranded RNA-stimulated polymerization of adenosine triphosphate in 2 '-5 ' oligoadenylates (2-5A), which can activate the latent RNase (RNase L) to degrade RNA. However, accumulated evidence over the years have suggested alternative mode of antiviral function of several OAS family proteins. Furthermore, recent studies have connected some OAS proteins with wider function beyond viral infection. Here, we review some of the canonical and noncanonical functions of OAS proteins and their mechanisms.

引用

页码：487 / 494

页数：8

共 104 条

[1] Genetic regulation of OAS1 nonsense-mediated decay underlies association with COVID-19 hospitalization in patients of European and African ancestries [J].

Banday, A. Rouf ;

Stanifer, Megan L. ;

Florez-Vargas, Oscar ;

Onabajo, Olusegun O. ;

Papenberg, Brenen W. ;

Zahoor, Muhammad A. ;

Mirabello, Lisa ;

Ring, Timothy J. ;

Lee, Chia-Han ;

Albert, Paul S. ;

Andreakos, Evangelos ;

Arons, Evgeny ;

Barsh, Greg ;

Biesecker, Leslie G. ;

Boyle, David L. ;

Brahier, Mark S. ;

Burnett-Hartman, Andrea ;

Carrington, Mary ;

Chang, Euijin ;

Choe, Pyoeng Gyun ;

Chisholm, Rex L. ;

Colli, Leandro M. ;

Dalgard, Clifton L. ;

Dude, Carolynn M. ;

Edberg, Jeff ;

Erdmann, Nathan ;

Feigelson, Heather S. ;

Fonseca, Benedito A. ;

Firestein, Gary S. ;

Gehring, Adam J. ;

Guo, Cuncai ;

Ho, Michelle ;

Holland, Steven ;

Hutchinson, Amy A. ;

Im, Hogune ;

Irby, Les'Shon ;

Ison, Michael G. ;

Joseph, Naima T. ;

Kim, Hong Bin ;

Kreitman, Robert J. ;

Korf, Bruce R. ;

Lipkin, Steven M. ;

Mahgoub, Siham M. ;

Mohammed, Iman ;

Paschoalini, Guilherme L. ;

Pacheco, Jennifer A. ;

Peluso, Michael J. ;

Rader, Daniel J. ;

Redden, David T. ;

Ritchie, Marylyn D. .

NATURE GENETICS, 2022, 54 (08) :1103-+

[2] OAS-RNase L innate immune pathway mediates the cytotoxicity of a DNA-demethylating drug [J].

Banerjee, Shuvojit ;

Gusho, Elona ;

Gaughan, Christina ;

Dong, Beihua ;

Gu, Xiaorong ;

Holvey-Bates, Elise ;

Talukdar, Manisha ;

Li, Yize ;

Weiss, Susan R. ;

Sicheri, Frank ;

Saunthararajah, Yogen ;

Stark, George R. ;

Silverman, Robert H. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2019, 116 (11) :5071-5076

[3] Opposing Functions of Interferon Coordinate Adaptive and Innate Immune Responses to Cancer Immune Checkpoint Blockade [J].

Benci, Joseph L. ;

Johnson, Lexus R. ;

Choa, Ruth ;

Xu, Yuanming ;

Qiu, Jingya ;

Zhou, Zilu ;

Xu, Bihui ;

Ye, Darwin ;

Nathanson, Katherine L. ;

June, Carl H. ;

Wherry, E. John ;

Zhang, Nancy R. ;

Ishwaran, Hemant ;

Hellmann, Matthew D. ;

Wolchok, Jedd D. ;

Kambayashi, Taku ;

Minn, Andy J. .

CELL, 2019, 178 (04) :933-+

[4] OAS1/RNase L executes RIG-I ligand-dependent tumor cell apoptosis [J].

Boehmer, Daniel F. R. ;

Formisano, Simone ;

Mann, Carina C. de Oliveira ;

Mueller, Stephan A. ;

Kluge, Michael ;

Metzger, Philipp ;

Rohlfs, Meino ;

Hoerth, Christine ;

Kocheise, Lorenz ;

Lichtenthaler, Stefan F. ;

Hopfner, Karl-Peter ;

Endres, Stefan ;

Rothenfusser, Simon ;

Friedel, Caroline C. ;

Duewell, Peter ;

Schnurr, Max ;

Koenig, Lars M. .

SCIENCE IMMUNOLOGY, 2021, 6 (61)

[5] Variation in antiviral 2′,5′-oligoadenylate synthetase (2′5′AS) enzyme activity is controlled by a single-nucleotide polymorphism at a splice-acceptor site in the OAS1 gene [J].

Bonnevie-Nielsen, V ;

Field, LL ;

Lu, S ;

Zheng, DJ ;

Li, M ;

Martensen, PM ;

Nielsen, TB ;

Beck-Nielsen, H ;

Lau, YL ;

Pociot, F .

AMERICAN JOURNAL OF HUMAN GENETICS, 2005, 76 (04) :623-633

[6] The Roles of Type I Interferon in Bacterial Infection [J].

Boxx, Gayle M. ;

Cheng, Genhong .

CELL HOST & MICROBE, 2016, 19 (06) :760-769

[7] The large form of human 2′,5′-Oligoadenylate Synthetase (OAS3) exerts antiviral effect against Chikungunya virus [J].

Brehin, Anne-Claire ;

Casademont, Isabelle ;

Frenkiel, Marie-Pascale ;

Julier, Cecile ;

Sakuntabhai, Anavaj ;

Despres, Philippe .

VIROLOGY, 2009, 384 (01) :216-222

[8] The interferon-stimulated gene product oligoadenylate synthetase-like protein enhances replication of Kaposi's sarcoma-associated herpesvirus (KSHV) and interacts with the KSHV ORF20 protein [J].

Bussey, Kendra A. ;

Lau, Ulrike ;

Schumann, Sophie ;

Gallo, Antonio ;

Osbelt, Lisa ;

Stempel, Markus ;

Arnold, Christine ;

Wissing, Josef ;

Gad, Hans Henrik ;

Hartmann, Rune ;

Brune, Wolfram ;

Jaensch, Lothar ;

Whitehouse, Adrian ;

Brinkmann, Melanie M. .

PLOS PATHOGENS, 2018, 14 (03)

[9] Association analysis of polymorphisms in OAS1 with susceptibility and severity of hand, foot and mouth disease [J].

Cai, Y. ;

Chen, Q. ;

Zhou, W. ;

Chu, C. ;

Ji, W. ;

Ding, Y. ;

Xu, J. ;

Ji, Z. ;

You, H. ;

Wang, J. .

INTERNATIONAL JOURNAL OF IMMUNOGENETICS, 2014, 41 (05) :384-392

[10] Recurrent Loss-of-Function Mutations Reveal Costs to OAS1 Antiviral Activity in Primates [J].

Carey, Clayton M. ;

Govande, Apurva A. ;

Cooper, Juliane M. ;

Hartley, Melissa K. ;

Kranzusch, Philip J. ;

Elde, Nels C. .

CELL HOST & MICROBE, 2019, 25 (02) :336-+

← 1 2 3 4 5 6 7 8 9 10 →