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Structural insight into HIV-1 capsid recognition by rhesus TRIM5α.

Yang H, Ji X, Zhao G, Ning J, Zhao Q, Aiken C, Gronenborn AM, Zhang P, Xiong Y
Proc Natl Acad Sci U S A 109 18372-7 (2012)
Cited: 49 times
EuropePMC logo PMID: 23091002

Abstract

Tripartite motif protein isoform 5 alpha (TRIM5α) is a potent antiviral protein that restricts infection by HIV-1 and other retroviruses. TRIM5α recognizes the lattice of the retrovirus capsid through its B30.2 (PRY/SPRY) domain in a species-specific manner. Upon binding, TRIM5α induces premature disassembly of the viral capsid and activates the downstream innate immune response. We have determined the crystal structure of the rhesus TRIM5α PRY/SPRY domain that reveals essential features for capsid binding. Combined cryo-electron microscopy and biochemical data show that the monomeric rhesus TRIM5α PRY/SPRY, but not the human TRIM5α PRY/SPRY, can bind to HIV-1 capsid protein assemblies without causing disruption of the capsid. This suggests that the PRY/SPRY domain alone constitutes an important pattern-sensing component of TRIM5α that is capable of interacting with viral capsids of different curvatures. Our results provide molecular insights into the mechanisms of TRIM5α-mediated retroviral restriction.

Reviews - 4b3n mentioned but not cited (2)

  1. HIV suppression by host restriction factors and viral immune evasion. Jia X, Zhao Q, Xiong Y. Curr Opin Struct Biol 31 106-114 (2015)
  2. Crystal structures of MBP fusion proteins. Waugh DS. Protein Sci 25 559-571 (2016)

Articles - 4b3n mentioned but not cited (2)



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  1. Classification of intrinsically disordered regions and proteins. van der Lee R, Buljan M, Lang B, Weatheritt RJ, Daughdrill GW, Dunker AK, Fuxreiter M, Gough J, Gsponer J, Jones DT, Kim PM, Kriwacki RW, Oldfield CJ, Pappu RV, Tompa P, Uversky VN, Wright PE, Babu MM. Chem Rev 114 6589-6631 (2014)
  2. Molecular basis of human immunodeficiency virus type 1 drug resistance: overview and recent developments. Menéndez-Arias L. Antiviral Res 98 93-120 (2013)
  3. Restriction of HIV-1 and other retroviruses by TRIM5. Ganser-Pornillos BK, Pornillos O. Nat Rev Microbiol 17 546-556 (2019)
  4. Capsid-binding retrovirus restriction factors: discovery, restriction specificity and implications for the development of novel therapeutics. Sanz-Ramos M, Stoye JP. J Gen Virol 94 2587-2598 (2013)
  5. Roles of HIV-1 capsid in viral replication and immune evasion. Le Sage V, Mouland AJ, Valiente-Echeverría F. Virus Res 193 116-129 (2014)
  6. Conserved structural and functional aspects of the tripartite motif gene family point towards therapeutic applications in multiple diseases. Gushchina LV, Kwiatkowski TA, Bhattacharya S, Weisleder NL. Pharmacol Ther 185 12-25 (2018)
  7. Molecular Architecture of the Retroviral Capsid. Perilla JR, Gronenborn AM. Trends Biochem Sci 41 410-420 (2016)
  8. Host Restriction Factors and Human Immunodeficiency Virus (HIV-1): A Dynamic Interplay Involving All Phases of the Viral Life Cycle. D Urbano V, De Crignis E, Re MC. Curr HIV Res 16 184-207 (2018)
  9. HIV-1 capsid variability: viral exploitation and evasion of capsid-binding molecules. Saito A, Yamashita M. Retrovirology 18 32 (2021)
  10. Visualizing HIV-1 Capsid and Its Interactions with Antivirals and Host Factors. Wilbourne M, Zhang P. Viruses 13 246 (2021)
  11. Using TRIM5α as an HIV therapeutic: the alpha gene? Anderson JS. Expert Opin Biol Ther 13 1029-1038 (2013)
  12. Updating on Roles of HIV Intrinsic Factors: A Review of Their Antiviral Mechanisms and Emerging Functions. Hadpech S, Moonmuang S, Chupradit K, Yasamut U, Tayapiwatana C. Intervirology 65 67-79 (2022)
  13. HIV-1 capsid and viral DNA integration. Dwivedi R, Prakash P, Kumbhar BV, Balasubramaniam M, Dash C. mBio 15 e0021222 (2024)

Articles citing this publication (32)



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