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RaPID Analysis of Cytomegalovirus of Long Noncoding RNA Binding Proteins
Author(s) -
Lee Jessica E.,
Kulesza Caroline
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.460.7
Subject(s) - rna , biology , human cytomegalovirus , cytomegalovirus , computational biology , rna binding protein , virology , virus , microbiology and biotechnology , genetics , gene , herpesviridae , viral disease
Human Cytomegalovirus (HCMV) is a ubiquitous herpes virus that is widespread and usually asymptomatic among healthy individuals. Congenital HCMV infections are the leading cause of virally induced birth defects. HCMV also causes severe disease in immunocompromised patients. Previous work in our laboratory has shown that CMV encodes a large noncoding RNA called RNA5.0. Using an animal model, the homologous RNA in the murine model called RNA7.2 has been shown to help the virus persist in host salivary glands, but it is unclear how this works at the molecular level. To identify the proteins attaching to RNA5.0, the RaPID system will be used. The RaPID system uses a highly active biotin ligase that tags proteins which bind to specific RNA sequences in cells. The RaPID system was pioneered in Paul Khavari's lab to demonstrate a small cellular RNA (EDEN15) binds to the CELF1 protein. We have reproduced their data in our laboratory and will use this system to identify RNA5.0 binding proteins. We will be looking for proteins that bind to the 3′ end of RNA5.0 because there is evidence this sequence is related to processing and stability of the RNA. Moving forward different length fragments spanning the 3′ end of RNA5.0 will be used in the RaPID system to identify which proteins interact with the sequence. The identified proteins might point out specific pathways to target for a potential treatment for CMV. This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .