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Cyclophilin, TRIM5, and innate immunity to HIV-1.

The peptidyl-prolyl isomerase cyclophilin A (CypA) binds a proline-rich loop on the surface of HIV-1 capsid (CA). This interaction increases HIV-1 infectivity in humans but promotes an anti-HIV-1 restriction activity in non-human primates. Efforts to understand these paradoxical effects of cyclophilin, along with more targeted approaches to uncover the genetic basis for HIV-1 restriction, led to the discovery of TRIM5 (tripartite motif protein 5), a CA-specific receptor for the retroviral core. The ensuing TRIM5 publication flurry established a paradigm of innate immunity in which the protein lattice of an invading retroviral core, rather than double-stranded RNA or lipopolysaccharide, is recognized by a multimeric, cytoplasmic receptor. CypA modulates HIV-1 virion core detection by this class of innate pattern recognition molecule, apparently by inducing subtle shifts in CA conformation.[1]

References

  1. Cyclophilin, TRIM5, and innate immunity to HIV-1. Sokolskaja, E., Luban, J. Curr. Opin. Microbiol. (2006) [Pubmed]
 
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