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Cited by 28RNA Research and SplicingHIV Research and TreatmentRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

HIV-1 and two avian retroviral 5′ untranslated regions bind orthologous human and chicken RNA binding proteins

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Stake, Matthew, Singh, Deepali, Singh, Gatikrushna, Marcela Hernandez, J., Kaddis Maldonado, Rebecca, Parent, Leslie J., Boris-Lawrie, Kathleen·2015·Virology
DOI 10.1016/j.virol.2015.06.001PMC PMC4877169
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Abstract

Essential host cofactors in retrovirus replication bind cis-acting sequences in the 5'untranslated region (UTR). Although host RBPs are crucial to all aspects of virus biology, elucidating their roles in replication remains a challenge to the field. Here RNA affinity-coupled-proteomics generated a comprehensive, unbiased inventory of human and avian RNA binding proteins (RBPs) co-isolating with 5'UTRs of HIV-1, spleen necrosis virus and Rous sarcoma virus. Applying stringent biochemical and statistical criteria, we identified 185 RBP; 122 were previously implicated in retrovirus biology and 63 are new to the 5'UTR proteome. RNA electrophoretic mobility assays investigated paralogs present in the common ancestor of vertebrates and one hnRNP was identified as a central node to the biological process-anchored networks of HIV-1, SNV, and RSV 5' UTR-proteomes. This comprehensive view of the host constituents of retroviral RNPs is broadly applicable to investigation of viral replication and antiviral response in both human and avian cell lineages.

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  • Cellular factors interacting with HIV-1 proteins and RNAs have been identified using proteomic approaches.

    “In recent years, cellular factors interacting with HIV-1 proteins and RNAs have been identified using proteomic approaches (122-124).”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [123]

  • Human EPRS and ArgRS bind to the HIV-1 5'UTR, and avian LysRS and SerRS bind to the 5'UTR of RSV.

    “Interestingly, human EPRS and ArgRS bind to the HIV-1 5ЈUTR, and avian LysRS and SerRS bind to the 5ЈUTR of RSV (Table 1).”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [123]

    The Introduction and Results §3.1 report human and chicken proteins co-isolating with the HIV-1 and RSV 5′ UTRs, but the passages do not identify the four proteins in the claim. Searches for EPRS, ArgRS, LysRS, and SerRS found no passage confirming their respective pairings with those UTRs. (LLM, conf=0.72)

    Experimental — accuracy not yet measured

  • LeuRS interacts with unspliced full-length HIV-1 RNA.

    “| Interacts with unspliced full-length HIV-1 RNA | LeuRS a | 123 |”

    From Role of host tRNAs and aminoacyl-tRNA synthetases in retroviral replication (2019) · cites this paper as [123]

    The Results (§3.1; page unavailable) describe affinity experiments using HIV-1 5′ UTR fragments, not unspliced full-length HIV-1 RNA. Searches for LeuRS, leucyl-tRNA synthetase, and LARS found no passage in our copy linking that protein to HIV-1 RNA. (LLM, conf=0.75)

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Metadata

Authors
Stake, M., Singh, D., Singh, G., Marcela Hernandez, J., Kaddis Maldonado, R., Parent, L. J., & Boris-Lawrie, K.
Affiliations
  • Pennsylvania State University (US)
  • Gautam Buddha University (IN)
  • University of Minnesota (US)
ORCID
Venue
Virology
Publisher
Elsevier BV
Published
2015-12
Volume
486
Pages
307-320
ISSN
0042-6822 (ISSN-L)
DOI
10.1016/j.virol.2015.06.001
PMC
PMC4877169
OpenAlex
W2173915105
Cited by
28
References
2
Citations by year
2025: 1 · 2024: 4 · 2023: 2 · 2022: 3 · 2021: 2 · 2020: 4 · 2019: 4 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 1
FWCI
1.16
Type
journal article
Language
en
Open access
Licence
Locations
  • Virology (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health’s National Institutes of General Medical Sciences (P50GM103297)
  • LJP
  • KBL
  • National Cancer Institute (P01CA16058)
  • The Ohio State University Comprehensive Cancer Center
  • NIH National Cancer Institute (LJP (R01 CA76534), RJK (F31 CA171862))
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
HIV-1, avian retroviruses, 5' untranslated region, RNA-binding proteins, spleen necrosis virus, Rous sarcoma virus, protein-RNA complex, heterogeneous nuclear ribonucleoproteins, host-virus interaction, human
MeSH terms
Amino Acid Sequence, Animals, Chickens, Humans, Molecular Sequence Data, Poultry Diseases, Retroviridae, Retroviridae Infections, RNA, Viral, HIV-1, HIV Infections, RNA-Binding Proteins, 5' Untranslated Regions

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