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Specific interaction of HeLa cell proteins with coxsackievirus B3 3'UTR: La autoantigen binds the 3' and 5'UTR independently of the poly(A) tail.
Cell Microbiol. 2007 Jul; 9(7):1705-15.CM

Abstract

Coxsackievirus B3 (CVB3) is a positive, single-stranded RNA virus. The secondary structure of the 3' untranslated region (3'UTR) of CVB3 RNA consists of three stem-loops and is followed by a poly(A) tail sequence. These stem-loop structures have been suggested to participate in the regulation of viral replication through interaction with cellular proteins that are yet to be identified. In this study, by competitive UV cross-linking using mutated 3'UTR probes we have demonstrated that the poly(A) tail is essential for promoting HeLa cell protein interactions with the 3'UTR because deletion of this sequence abolished most of the protein interactions. Unexpectedly, mutations that disrupted the tertiary loop-loop interactions without affecting the stem-loops did not apparently affect these protein interactions, indicating that secondary structure rather than the high-order structure may play a major role in recruiting these RNA binding proteins. Among the observed 3'UTR RNA binding proteins, we have confirmed a 52 kDa protein as the human La autoantigen by using purified recombinant protein and a polyclonal La antibody. This protein can interact with both the 3' and 5'UTRs independently of the poly(A) tail. Further analysis by two-stage UV cross-linking, we found that the 3' and 5'UTR sequences may share the same binding site on the La protein.

Authors+Show Affiliations

Department of Pathology and Laboratory Medicine, The James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research, University of British Columbia-St. Paul's Hospital, Vancouver, British Columbia, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17346312

Citation

Cheung, Paul, et al. "Specific Interaction of HeLa Cell Proteins With Coxsackievirus B3 3'UTR: La Autoantigen Binds the 3' and 5'UTR Independently of the poly(A) Tail." Cellular Microbiology, vol. 9, no. 7, 2007, pp. 1705-15.
Cheung P, Lim T, Yuan J, et al. Specific interaction of HeLa cell proteins with coxsackievirus B3 3'UTR: La autoantigen binds the 3' and 5'UTR independently of the poly(A) tail. Cell Microbiol. 2007;9(7):1705-15.
Cheung, P., Lim, T., Yuan, J., Zhang, M., Chau, D., McManus, B., & Yang, D. (2007). Specific interaction of HeLa cell proteins with coxsackievirus B3 3'UTR: La autoantigen binds the 3' and 5'UTR independently of the poly(A) tail. Cellular Microbiology, 9(7), 1705-15.
Cheung P, et al. Specific Interaction of HeLa Cell Proteins With Coxsackievirus B3 3'UTR: La Autoantigen Binds the 3' and 5'UTR Independently of the poly(A) Tail. Cell Microbiol. 2007;9(7):1705-15. PubMed PMID: 17346312.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Specific interaction of HeLa cell proteins with coxsackievirus B3 3'UTR: La autoantigen binds the 3' and 5'UTR independently of the poly(A) tail. AU - Cheung,Paul, AU - Lim,Travis, AU - Yuan,Jane, AU - Zhang,Mary, AU - Chau,David, AU - McManus,Bruce, AU - Yang,Decheng, Y1 - 2007/03/08/ PY - 2007/3/10/pubmed PY - 2007/8/22/medline PY - 2007/3/10/entrez SP - 1705 EP - 15 JF - Cellular microbiology JO - Cell Microbiol VL - 9 IS - 7 N2 - Coxsackievirus B3 (CVB3) is a positive, single-stranded RNA virus. The secondary structure of the 3' untranslated region (3'UTR) of CVB3 RNA consists of three stem-loops and is followed by a poly(A) tail sequence. These stem-loop structures have been suggested to participate in the regulation of viral replication through interaction with cellular proteins that are yet to be identified. In this study, by competitive UV cross-linking using mutated 3'UTR probes we have demonstrated that the poly(A) tail is essential for promoting HeLa cell protein interactions with the 3'UTR because deletion of this sequence abolished most of the protein interactions. Unexpectedly, mutations that disrupted the tertiary loop-loop interactions without affecting the stem-loops did not apparently affect these protein interactions, indicating that secondary structure rather than the high-order structure may play a major role in recruiting these RNA binding proteins. Among the observed 3'UTR RNA binding proteins, we have confirmed a 52 kDa protein as the human La autoantigen by using purified recombinant protein and a polyclonal La antibody. This protein can interact with both the 3' and 5'UTRs independently of the poly(A) tail. Further analysis by two-stage UV cross-linking, we found that the 3' and 5'UTR sequences may share the same binding site on the La protein. SN - 1462-5814 UR - https://www.unboundmedicine.com/medline/citation/17346312/Specific_interaction_of_HeLa_cell_proteins_with_coxsackievirus_B3_3'UTR:_La_autoantigen_binds_the_3'_and_5'UTR_independently_of_the_poly_A__tail_ L2 - https://doi.org/10.1111/j.1462-5822.2007.00904.x DB - PRIME DP - Unbound Medicine ER -