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John J Karijolich

John J Karijolich, Ph.D.

Assistant Professor of Pathology, Microbiology and Immunology

Contact Information:

A-4301 Medical Center North
1161 21st Ave
Nashville, TN 37232-2561
(615) 875-7686

Profile

Research in the Karijolich laboratory is focused on understanding host-virus interactions in the context of gammaherpesvirus infection. Gammaherpesviruses, which include the human oncogenic viruses Kaposi Sarcoma-associated herpesvirus (KSHV) and Epstein Barr virus (EBV), are a family of large double-stranded DNA lymphotrophic viruses that are the causative agents of a variety of disorders, including lymphoproliferative diseases, lymphomas, as well as other nonlymphoid cancers in mammals. Studies of the host response to viral infection have historically focused on protein-coding genes, thus our understanding of how the non-protein-coding transcriptome, including both viral- and host-derived noncoding RNAs, impacts host-virus interactions is limited. Along this line, our primary research goals are directed towards understanding how noncoding RNAs and their RNA-binding proteins are integrated in to the regulation of gene expression and modulation of the host immune response during gammaherpesvirus infection.

Education
 
  • Ph.D., University of Rochester, Rochester, New York
  • B.A., Biology, Ripon College, Ripon, Wisconsin
 
Research Description

The association between infection with viruses and neoplasia is well established for a variety of cancers. In fact, approximately 12% of human cancers worldwide are caused by oncogenic viral infections, with more than 80% of cases occurring in the developing world. Despite their prevalence and public health importance, our understanding and ability to manage viral-induced cancers is still limited. This is in part due to the complexity of host-virus interactions leading to cellular transformation.

Research in our laboratory is focused on defining the host-virus interaction in the context of gammaherpesviral infection. ¿-herpesviruses, which include the human oncogenic viruses Kaposi Sarcoma-associated herpesvirus (KSHV) and Epstein Barr virus (EBV), are a family of large double-stranded DNA lymphotrophic viruses that are the causative agents of a variety of disorders, including lymphoproliferative diseases, lymphomas, as well as other nonlymphoid cancers in mammals. Studies of the host response to viral infection have historically focused on protein-coding genes, thus our understanding of how the non-protein-coding transcriptome, including both viral- and host-derived noncoding RNAs, impacts host-virus interactions is limited. Along this line, our primary research goals are directed towards understanding how noncoding RNAs and their RNA-binding proteins are integrated in to the regulation of gene expression and modulation of the host immune response during ¿-herpesviral infection. To accomplish this we undertake a multidisciplinary approach combining virology, immunology, RNA biochemistry, proteomics, and genomics/transcriptomics. Major thematic questions of the lab include:

1) What are the endogenous and exogenous noncoding RNA species that contribute to innate immune modulation and how are these functions mediated?

2) How does the cell intrinsic innate immune system shape the ¿-herpesviral lifecycle and what are the host and viral entities at play?

3) What is the contribution of endogenous retroviruses and transposons to the host-virus interaction?

Publications
  • Karijolich J, Zhao Y, Alla R, Glaunsinger B. Genome-wide mapping of infection-induced SINE RNAs reveals a role in selective mRNA export. Nucleic Acids Res [print-electronic]. 2017 Mar 3/15/2017; PMID: 28334904, PII: 3071714, DOI: 10.1093/nar/gkx180, ISSN: 1362-4962.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/28334904.
  • Zhao Y, Karijolich J, Glaunsinger B, Zhou Q. Pseudouridylation of 7SK snRNA promotes 7SK snRNP formation to suppress HIV-1 transcription and escape from latency. EMBO Rep [print-electronic]. 2016 Aug 8/24/2016; PMID: 27558685, PII: embr.201642682, DOI: 10.15252/embr.201642682, ISSN: 1469-3178.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/27558685.
  • Huang C, Karijolich J, Yu YT. Detection and quantification of RNA 2'-O-methylation and pseudouridylation. Methods [print-electronic]. 2016 Jul 7/1/2016; 103: 68-76. PMID: 26853326, PMCID: PMC4921259, PII: S1046-2023(16)30021-4, DOI: 10.1016/j.ymeth.2016.02.003, ISSN: 1095-9130.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/26853326.
  • Karijolich J, Yi C, Yu YT. Transcriptome-wide dynamics of RNA pseudouridylation. Nat. Rev. Mol. Cell Biol [print-electronic]. 2015 Oct; 16(10): 581-5. PMID: 26285676, PII: nrm4040, DOI: 10.1038/nrm4040, ISSN: 1471-0080.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/26285676.
  • Karijolich J, Yu YT. The new era of RNA modification. RNA. 2015 Apr; 21(4): 659-60. PMID: 25780180, PMCID: PMC4371322, PII: 21/4/659, DOI: 10.1261/rna.049650.115, ISSN: 1469-9001.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/25780180.
  • Karijolich J, Abernathy E, Glaunsinger BA. Infection-Induced Retrotransposon-Derived Noncoding RNAs Enhance Herpesviral Gene Expression via the NF-¿B Pathway. PLoS Pathog. 2015; 11(11): e1005260. PMID: 26584434, PMCID: PMC4652899, PII: PPATHOGENS-D-15-02010, DOI: 10.1371/journal.ppat.1005260, ISSN: 1553-7374.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/26584434.
  • Karijolich J, Yu YT. Therapeutic suppression of premature termination codons: mechanisms and clinical considerations (review). Int. J. Mol. Med [print-electronic]. 2014 Aug; 34(2): 355-62. PMID: 24939317, PMCID: PMC4094583, DOI: 10.3892/ijmm.2014.1809, ISSN: 1791-244X.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/24939317.
  • Karijolich J, Zhao Y, Peterson B, Zhou Q, Glaunsinger B. Kaposi's sarcoma-associated herpesvirus ORF45 mediates transcriptional activation of the HIV-1 long terminal repeat via RSK2. J. Virol [print-electronic]. 2014 Jun; 88(12): 7024-35. PMID: 24719417, PMCID: PMC4054375, PII: JVI.00931-14, DOI: 10.1128/JVI.00931-14, ISSN: 1098-5514.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/24719417.
  • Lim SJ, Scott A, Xiong XP, Vahidpour S, Karijolich J, Guo D, Pei S, Yu YT, Zhou R, Li WX. Requirement for CRIF1 in RNA interference and Dicer-2 stability. RNA Biol. 2014; 11(9): 1171-9. PMID: 25483042, PMCID: PMC4615304, DOI: 10.4161/rna.34381, ISSN: 1555-8584.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/25483042.
  • Karijolich JJ, Hampsey M. The Mediator complex. Curr. Biol. 2012 Dec 12/18/2012; 22(24): R1030-1. PMID: 23257183, PII: S0960-9822(12)01320-6, DOI: 10.1016/j.cub.2012.11.011, ISSN: 1879-0445.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/23257183.
  • Karijolich J, Yu YT. Converting nonsense codons into sense codons by targeted pseudouridylation. Nature. 2011 Jun 6/16/2011; 474(7351): 395-8. PMID: 21677757, PMCID: PMC3381908, PII: nature10165, DOI: 10.1038/nature10165, ISSN: 1476-4687.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/21677757.
  • Huang C, Karijolich J, Yu YT. Post-transcriptional modification of RNAs by artificial Box H/ACA and Box C/D RNPs. Methods Mol. Biol. 2011; 718: 227-44. PMID: 21370052, PMCID: PMC4161979, DOI: 10.1007/978-1-61779-018-8_14, ISSN: 1940-6029.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/21370052.
  • Karijolich J, Yu YT. Spliceosomal snRNA modifications and their function. RNA Biol [print-electronic]. 2010 Mar; 7(2): 192-204. PMID: 20215871, PMCID: PMC4154345, PII: 11207, ISSN: 1555-8584.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/20215871.
  • Karijolich J, Kantartzis A, Yu YT. Quantitative analysis of RNA modifications. Methods Mol. Biol. 2010; 629: 21-32. PMID: 20387140, PMCID: PMC4154561, DOI: 10.1007/978-1-60761-657-3_2, ISSN: 1940-6029.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/20387140.
  • Karijolich J, Kantartzis A, Yu YT. RNA modifications: a mechanism that modulates gene expression. Methods Mol. Biol. 2010; 629: 1-19. PMID: 20387139, PMCID: PMC4154353, DOI: 10.1007/978-1-60761-657-3_1, ISSN: 1940-6029.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/20387139.
  • Karijolich J, Yu YT. Insight into the Protein Components of the Box H/ACA RNP. Curr Proteomics. 2008 Jul 7/1/2008; 5(2): 129-37. PMID: 19829749, PMCID: PMC2760984, DOI: 10.2174/157016408784911936, ISSN: 1570-1646.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/19829749.
  • Moelling C, Oberschlacke R, Ward P, Karijolich J, Borisova K, Bjelos N, Bergeron L. Metal-dependent repression of siderophore and biofilm formation in Actinomyces naeslundii. FEMS Microbiol. Lett [print-electronic]. 2007 Oct; 275(2): 214-20. PMID: 17825071, PII: FML888, DOI: 10.1111/j.1574-6968.2007.00888.x, ISSN: 0378-1097.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/17825071.
  • Karijolich J, Stephenson D, Yu YT. Biochemical purification of box H/ACA RNPs involved in pseudouridylation. Meth. Enzymol. 2007; 425: 241-62. PMID: 17673087, PII: S0076-6879(07)25011-6, DOI: 10.1016/S0076-6879(07)25011-6, ISSN: 0076-6879.
    Available from: http://www.ncbi.nlm.nih.gov/pubmed/17673087.