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. 2005 Apr;79(7):3930-7.
doi: 10.1128/JVI.79.7.3930-3937.2005.

Retrovirus restriction by TRIM5alpha variants from Old World and New World primates

Byeongwoon Song  1 , Hassan Javanbakht, Michel Perron, Do Hyun Park, Matthew Stremlau, Joseph Sodroski
Affiliations

Retrovirus restriction by TRIM5alpha variants from Old World and New World primates

Byeongwoon Song et al. J Virol. 2005 Apr.

Abstract

The TRIM5alpha proteins of humans and some Old World monkeys have been shown to block infection of particular retroviruses following virus entry into the host cell. Infection of most New World monkey cells by the simian immunodeficiency virus of macaques (SIVmac) is restricted at a similar point. Here we examine the antiretroviral activity of TRIM5alpha orthologs from humans, apes, Old World monkeys, and New World monkeys. Chimpanzee and orangutan TRIM5alpha proteins functionally resembled human TRIM5alpha, potently restricting infection by N-tropic murine leukemia virus (N-MLV) and moderately restricting human immunodeficiency virus type 1 (HIV-1) infection. Notably, TRIM5alpha proteins from several New World monkey species restricted infection by SIVmac and the SIV of African green monkeys, SIVagm. Spider monkey TRIM5alpha, which has an expanded B30.2 domain v3 region due to a tandem triplication, potently blocked infection by a range of retroviruses, including SIVmac, SIVagm, HIV-1, and N-MLV. Tandem duplications in the TRIM5alpha B30.2 domain v1 region of African green monkeys are also associated with broader antiretroviral activity. Thus, variation in TRIM5alpha proteins among primate species accounts for the observed patterns of postentry restrictions in cells from these animals. The TRIM5alpha proteins of some monkey species exhibit dramatic lengthening of particular B30.2 variable regions and an expanded range of susceptible retroviruses.

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Figures

FIG. 1.
FIG. 1.
Primate TRIM5α sequences. The primary amino acid sequences of the TRIM5α proteins studied herein are aligned. The primate species of origin are indicated to the left of the sequences (agm, African green monkey; pyg, subspecies pygerythrus; tan, subspecies tantalus; m., monkey). Amino acid residues that exhibit variation among the TRIM5α proteins are colored blue in the hominoids, green in the Old World monkeys, and red in the New World monkeys. Gaps in the sequence are indicated by dots. The boundaries of the RING, B-box 2, coiled-coil, and B30.2(SPRY) domains are indicated. The locations of variable regions (v1, v2, and v3) within the B30.2(SPRY) domain are indicated (33a). The tandemly duplicated sequences within the v1 regions of African green monkey TRIM5α proteins are underlined in green and black. The tandemly triplicated sequences in the TRIM5α protein of spider monkeys are underlined in red. The v4 variable region is not marked.
FIG. 1.
FIG. 1.
Primate TRIM5α sequences. The primary amino acid sequences of the TRIM5α proteins studied herein are aligned. The primate species of origin are indicated to the left of the sequences (agm, African green monkey; pyg, subspecies pygerythrus; tan, subspecies tantalus; m., monkey). Amino acid residues that exhibit variation among the TRIM5α proteins are colored blue in the hominoids, green in the Old World monkeys, and red in the New World monkeys. Gaps in the sequence are indicated by dots. The boundaries of the RING, B-box 2, coiled-coil, and B30.2(SPRY) domains are indicated. The locations of variable regions (v1, v2, and v3) within the B30.2(SPRY) domain are indicated (33a). The tandemly duplicated sequences within the v1 regions of African green monkey TRIM5α proteins are underlined in green and black. The tandemly triplicated sequences in the TRIM5α protein of spider monkeys are underlined in red. The v4 variable region is not marked.
FIG. 2.
FIG. 2.
Expression of the primate TRIM5α proteins. Lysates from HeLa cells stably expressing the indicated primate TRIM5α proteins, which contained HA epitope tags, were subjected to Western blotting with an antibody against HA. Control lysates from HeLa cells transduced with the empty pLPCX vector were analyzed in parallel (Vector). The major band corresponding to the TRIM5α protein is indicated by a white circle. The lysates were also Western blotted with an antibody directed against β-actin.
FIG. 3.
FIG. 3.
Effect of expression of the primate TRIM5α proteins on retrovirus infection. HeLa cells expressing TRIM5α proteins from the various primate species, or control HeLa cells transduced with the empty pLPCX vector (Vector), were incubated with the indicated recombinant viruses expressing GFP. Infected, GFP-positive cells were counted by FACS. The results of a typical experiment are shown. Similar results were obtained in three independent experiments. Hom, hominoid; OWM, Old World monkey; NWM, New World monkey.
FIG. 4.
FIG. 4.
Effect of expression of the primate TRIM5α proteins on infection of different MLVs. NIH3T3 cells expressing TRIM5α proteins from the various primate species, or control HeLa cells transduced with the empty pLPCX vector (Vector), were incubated with the indicated recombinant viruses expressing GFP. Infected, GFP-positive cells were counted by FACS. The results of a typical experiment are shown. Similar results were obtained in three independent experiments. Hom, hominoid; OWM, Old World monkey; NWM, New World monkey.
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