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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Retroviruses and retrotransposons both insert copies of their genetic elements into the genome of the host cell. Thus, the viral genes are passed on when the host genome is replicated or translated. A typical retroviral DNA sequence contains 3-4 genes that encode the different proteins required for its structural assembly and function as a molecular parasite. This DNA is transcribed into a single mRNA, which is very similar in structure to conventional mRNAs, i.e., it is capped at the 5’...
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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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As the name suggests, non-LTR retrotransposons lack the long terminal repeats characteristic of the LTR retrotransposons. Additionally, both LTR and non-LTR retrotransposons use distinct mechanisms of mobilization. Non-LTR retrotransposons are further divided into two classes - Long interspersed nuclear elements (LINEs) and short interspersed nuclear elements (SINEs), both of which occur abundantly in most mammals, including humans. Some of the active non-LTR retrotransposons in humans are L1...
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General Model for Retroviral Capsid Pattern Recognition by TRIM5 Proteins.

Jonathan M Wagner1, Devin E Christensen2, Akash Bhattacharya3

  • 1Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, Virginia, USA.

Journal of Virology
|December 1, 2017
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Summary

Both TRIM5α and TRIMCyp antiviral proteins use hexagonal lattice assembly for HIV-1 capsid recognition. This higher-order assembly mechanism is crucial for restriction, even for TRIMCyp which binds capsids with higher affinity.

Keywords:
pattern recognitionrestriction factorretrovirus

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Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Restriction factors are intrinsic cellular proteins that defend against microbial infections, including retroviruses like HIV-1.
  • TRIM5 proteins recognize the HIV-1 capsid, with TRIM5α requiring lattice assembly for sufficient avidity due to low-affinity binding.
  • TRIMCyp, an alternative TRIM5 homolog, binds HIV-1 capsids with higher affinity, leading to the hypothesis that it bypasses the need for assembly.

Purpose of the Study:

  • To investigate whether TRIMCyp, like TRIM5α, requires higher-order assembly for its antiviral activity against HIV-1.
  • To determine if TRIMCyp and TRIM5α share common mechanisms for HIV-1 capsid recognition and restriction.

Main Methods:

  • Analysis of TRIMCyp's self-association properties, specifically its B-box 2 domain.
  • Experimental assessment of TRIMCyp-mediated restriction of HIV-1 under stringent conditions.
  • Comparative analysis of TRIMCyp and TRIM5α assembly and binding mechanisms.

Main Results:

  • TRIMCyp's B-box 2 domain exhibits self-association capabilities, similar to TRIM5α, facilitating hexagonal lattice formation.
  • TRIMCyp-mediated restriction of HIV-1 was demonstrated to be dependent on this higher-order assembly.
  • Both TRIM5α and TRIMCyp utilize avidity-driven capsid pattern recognition through hexagonal lattice formation.

Conclusions:

  • Contrary to previous assumptions, TRIMCyp relies on higher-order hexagonal lattice assembly for effective HIV-1 restriction.
  • TRIM5α and TRIMCyp share a conserved mechanism of avidity-driven capsid recognition, highlighting a common evolutionary strategy for antiviral defense.
  • Understanding these assembly mechanisms provides insights into species-specific resistance to HIV-1.