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Purification and functional characterization of a biologically active full-length feline immunodeficiency virus (FIV) Pr50Gag

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Krishnan, Anjana, Pillai, Vineeta N., Chameettachal, Akhil, Mohamed Ali, Lizna, Nuzra Nagoor Pitchai, Fathima, Tariq, Saeed, Mustafa, Farah, Marquet, Roland +1 more·2019·Viruses
DOI 10.3390/v11080689PMC PMC6723490
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Abstract

The feline immunodeficiency virus (FIV) full-length Pr50Gag precursor is a key player in the assembly of new viral particles. It is also a critical component of the efficient selection and packaging of two copies of genomic RNA (gRNA) into the newly formed virus particles from a wide pool of cellular and spliced viral RNA. To understand the molecular mechanisms involved during FIV gRNA packaging, we expressed the His6-tagged and untagged recombinant FIV Pr50Gag protein both in eukaryotic and prokaryotic cells. The recombinant Pr50Gag-His6-tag fusion protein was purified from soluble fractions of prokaryotic cultures using immobilized metal affinity chromatography (IMAC). This purified protein was able to assemble in vitro into virus-like particles (VLPs), indicating that it preserved its ability to oligomerize/multimerize. Furthermore, VLPs formed in eukaryotic cells by the FIV full-length Pr50Gag both in the presence and absence of His6-tag could package FIV sub-genomic RNA to similar levels, suggesting that the biological activity of the recombinant full-length Pr50Gag fusion protein was retained in the presence of His6-tag at the carboxy terminus. Successful expression and purification of a biologically active, recombinant full-length Pr50Gag-His6-tag fusion protein will allow study of the intricate RNA-protein interactions involved during FIV gRNA encapsidation.

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  • Even in the absence of other viral components, especially PR, expressing MMTV, FIV, and SIV Gag polyproteins independently directs the virus to the appropriate assembly pathway.

    “Even in the absence of other viral components, especially PR, expressing MMTV, FIV, and SIV Gag polyproteins independently directs the virus to the appropriate assembly pathway”

    From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Krishnan et al. 2019

    The Introduction states that expressing FIV gag alone produces immature virus-like particles, supporting assembly without other viral components, including protease. It also describes MMTV as assembling intracellularly, but does not establish that independently expressed MMTV or SIV Gag follows its appropriate assembly pathway. (LLM, conf=0.82)

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Authors
Krishnan, A., Pillai, V. N., Chameettachal, A., Mohamed Ali, L., Nuzra Nagoor Pitchai, F., Tariq, S., Mustafa, F., Marquet, R., & A. Rizvi, T.
Affiliations
  • United Arab Emirates University (AE)
  • Department of Microbiology & Immunology, College of Medicine and Health Sciences (CMHS), United Arab Emirates University (UAEU), Al Ain 2000, UAE
  • Centre National de la Recherche Scientifique (FR)
ORCID
Venue
Viruses
Publisher
MDPI AG
Published
2019-07-27
Volume
11
Issue
8
Pages
689
ISSN
1999-4915 (ISSN-L)
DOI
10.3390/v11080689
PMC
PMC6723490
OpenAlex
W2966116102
Cited by
12
References
4
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2023: 2 · 2022: 1 · 2021: 3 · 2020: 1 · 2018: 1
FWCI
0.70
Type
journal article
Language
en
Open access
Licence
Locations
  • Viruses (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, cc-by)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • United Arab Emirates University (UCBR-31R143, UCBR 31R123 and UPAR-31M233)
  • College of Medicine and Health Sciences, United Arab Emirates University (31M280 and 31M388)
Topics
  • Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Virus-based gene therapy research
Keywords
feline immunodeficiency virus, Gag protein, recombinant protein purification, virus-like particles, viral RNA packaging, RNA-protein interactions, viral assembly, protein oligomerization
MeSH terms
Animals, Cats, Escherichia coli, Humans, Recombinant Proteins, RNA, Viral, Gene Products, gag, Gene Expression, Immunodeficiency Virus, Feline, Genome, Viral, Virus Assembly, HEK293 Cells

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