Novel Trim5 And Trimcyp Isoforms Of Old World Primates.

Overview

TRIM5alpha mediates a post-entry block to retroviral infection in Old World primates, while in Aotus trivirgatus this restriction is mediated by TRIMCyp. Both proteins encode N-terminal RING, B-box, and coiled coil domains; however, at the C-terminus TRIM5alpha encodes a B30.2 domain, while TRIMCyp encodes a CypA domain. The anti-viral activity mediated by TRIM5 proteins exhibits significant interspecies variability in anti-retroviral activity. Unlike most non-human primates, Macaca nemestrina can be infected ...
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Overview

TRIM5alpha mediates a post-entry block to retroviral infection in Old World primates, while in Aotus trivirgatus this restriction is mediated by TRIMCyp. Both proteins encode N-terminal RING, B-box, and coiled coil domains; however, at the C-terminus TRIM5alpha encodes a B30.2 domain, while TRIMCyp encodes a CypA domain. The anti-viral activity mediated by TRIM5 proteins exhibits significant interspecies variability in anti-retroviral activity. Unlike most non-human primates, Macaca nemestrina can be infected with HIV, suggesting that M. nemestrina TRIM5 proteins don't efficiently restrict these viruses. The M. nemestrina TRIM5 expression profile was defined in these animals by TRIM5-specific RT-PCR using PBMC total RNA. We identified a G to T SNP disrupting the intron 6 splice acceptor fixed in the M. nemestrina TRIM5 gene. This SNP is associated with the transcription of two novel TRIM5 isoforms in M. nemestrina. TRIM5theta encodes a two nucleotide deletion immediately downstream of the G to T SNP which truncates the protein before the B30.2/SPRY domain. TRIM5eta restores the original open reading frame by deleting all of exon 7. We also identified multiple TRIMCyp transcripts expressed by both M. nemestrina and M. fascicularis . One of these transcripts is predicted to express a full length TRIMCyp in which the CypA gene is fused to TRIM5 exon 6. CrFK cells were stably transduced with each protein and challenged with either HIV-1 NL4-3 or SIVmac239. As expected, none of the isoforms tested restricted SIVmac239 replication, and TRIM5theta does not restrict HIV-1 in vitro. TRIM5eta does not restrict HIV-1, suggesting the N-terminal alpha-helix encoded by exon 7 may play a significant role in restriction. Neither M. nemestrina nor M. fascicularis TRIMCyp restrict HIV-1. The independent evolution of TRIMCyp in Old World and New World primates indicates this protein provides an evolutionary advantage; to these animals. This work is the first to identify the co-transcription of TRIM5 and TRIMCyp in the same animal. In other systems, such as Fv1, co-expression of related anti-viral proteins significantly changes the anti-viral phenotype compared to the individual proteins. In these animals, therefore, it is possible that TRIM5 and TRIMCyp co-expression will modify or refine the primate retroviral restriction repertoire.
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Product Details

  • ISBN-13: 9781243546319
  • Publisher: BiblioLabsII
  • Publication date: 9/3/2011
  • Pages: 94
  • Product dimensions: 7.44 (w) x 9.69 (h) x 0.19 (d)

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