» Articles » PMID: 26797637

Exploiting TRNAs to Boost Virulence

Overview
Journal Life (Basel)
Specialty Biology
Date 2016 Jan 23
PMID 26797637
Citations 24
Authors
Affiliations
Soon will be listed here.
Abstract

Transfer RNAs (tRNAs) are powerful small RNA entities that are used to translate nucleotide language of genes into the amino acid language of proteins. Their near-uniform length and tertiary structure as well as their high nucleotide similarity and post-transcriptional modifications have made it difficult to characterize individual species quantitatively. However, due to the central role of the tRNA pool in protein biosynthesis as well as newly emerging roles played by tRNAs, their quantitative assessment yields important information, particularly relevant for virus research. Viruses which depend on the host protein expression machinery have evolved various strategies to optimize tRNA usage-either by adapting to the host codon usage or encoding their own tRNAs. Additionally, several viruses bear tRNA-like elements (TLE) in the 5'- and 3'-UTR of their mRNAs. There are different hypotheses concerning the manner in which such structures boost viral protein expression. Furthermore, retroviruses use special tRNAs for packaging and initiating reverse transcription of their genetic material. Since there is a strong specificity of different viruses towards certain tRNAs, different strategies for recruitment are employed. Interestingly, modifications on tRNAs strongly impact their functionality in viruses. Here, we review those intersection points between virus and tRNA research and describe methods for assessing the tRNA pool in terms of concentration, aminoacylation and modification.

Citing Articles

A virally encoded tRNA neutralizes the PARIS antiviral defence system.

Burman N, Belukhina S, Depardieu F, Wilkinson R, Skutel M, Santiago-Frangos A Nature. 2024; 634(8033):424-431.

PMID: 39111359 PMC: 11464382. DOI: 10.1038/s41586-024-07874-3.


Biological and genomic characterization of three psychrophilic phages.

Hammerl J, Pham M, El-Ahmad S, Manta D, Jackel C, Hertwig S Front Microbiol. 2024; 15:1423610.

PMID: 39056006 PMC: 11269248. DOI: 10.3389/fmicb.2024.1423610.


Viral proteins activate PARIS-mediated tRNA degradation and viral tRNAs rescue infection.

Burman N, Belukhina S, Depardieu F, Wilkinson R, Skutel M, Santiago-Frangos A bioRxiv. 2024; .

PMID: 38260645 PMC: 10802454. DOI: 10.1101/2024.01.02.573894.


Appelmans protocol - A directed in vitro evolution enables induction and recombination of prophages with expanded host range.

Vu T, Clark J, Jang E, DSouza R, Nguyen L, Pinto N Virus Res. 2023; 339:199272.

PMID: 37981215 PMC: 10730860. DOI: 10.1016/j.virusres.2023.199272.


Combination of genetically diverse Pseudomonas phages enhances the cocktail efficiency against bacteria.

Naknaen A, Samernate T, Wannasrichan W, Surachat K, Nonejuie P, Chaikeeratisak V Sci Rep. 2023; 13(1):8921.

PMID: 37264114 PMC: 10235106. DOI: 10.1038/s41598-023-36034-2.


References
1.
Xiao X, Hall C, Agris P . The design of a peptide sequence to inhibit HIV replication: a search algorithm combining Monte Carlo and self-consistent mean field techniques. J Biomol Struct Dyn. 2013; 32(10):1523-36. DOI: 10.1080/07391102.2013.825757. View

2.
Graham W, Barley-Maloney L, Stark C, Kaur A, Stolarchuk C, Stolyarchuk K . Functional recognition of the modified human tRNALys3(UUU) anticodon domain by HIV's nucleocapsid protein and a peptide mimic. J Mol Biol. 2011; 410(4):698-715. PMC: 3662833. DOI: 10.1016/j.jmb.2011.04.025. View

3.
Fernandez I, Bai X, Murshudov G, Scheres S, Ramakrishnan V . Initiation of translation by cricket paralysis virus IRES requires its translocation in the ribosome. Cell. 2014; 157(4):823-31. PMC: 4017093. DOI: 10.1016/j.cell.2014.04.015. View

4.
Mans R, Pleij C, Bosch L . tRNA-like structures. Structure, function and evolutionary significance. Eur J Biochem. 1991; 201(2):303-24. DOI: 10.1111/j.1432-1033.1991.tb16288.x. View

5.
Amitsur M, Levitz R, Kaufmann G . Bacteriophage T4 anticodon nuclease, polynucleotide kinase and RNA ligase reprocess the host lysine tRNA. EMBO J. 1987; 6(8):2499-503. PMC: 553660. DOI: 10.1002/j.1460-2075.1987.tb02532.x. View