title: Unique features of TRIM5alpha among closely related human TRIM family members.
abstract: The tripartite motif (TRIM) protein, TRIM5alpha, restricts some retroviruses, including human immunodeficiency virus (HIV-1), from infecting the cells of particular species. TRIM proteins contain RING, B-box, coiled-coil and, in some cases, B30.2(SPRY) domains. We investigated the properties of human TRIM family members closely related to TRIM5. These TRIM proteins, like TRIM5alpha, assembled into homotrimers and co-localized in the cytoplasm with TRIM5alpha. TRIM5alpha turned over more rapidly than related TRIM proteins. TRIM5alpha, TRIM34 and TRIM6 associated with HIV-1 capsid-nucleocapsid complexes assembled in vitro; the TRIM5alpha and TRIM34 interactions with these complexes were dependent on their B30.2(SPRY) domains. Only TRIM5alpha potently restricted infection by the retroviruses studied; overexpression of TRIM34 resulted in modest inhibition of simian immunodeficiency virus (SIV(mac)) infection. In contrast to the other TRIM genes examined, TRIM5 exhibited evidence of positive selection. The unique features of TRIM5alpha among its TRIM relatives underscore its special status as an antiviral factor.
authors.affiliation: Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Division of AIDS, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Xing
authors.initials: X
authors.lastname: Li
authors.forename: Bert
authors.initials: B
authors.lastname: Gold
authors.forename: Colm
authors.initials: C
authors.lastname: O'hUigin
authors.forename: Felipe
authors.initials: F
authors.lastname: Diaz-Griffero
authors.forename: Byeongwoon
authors.initials: B
authors.lastname: Song
authors.forename: Zhihai
authors.initials: Z
authors.lastname: Si
authors.forename: Yuan
authors.initials: Y
authors.lastname: Li
authors.forename: Wen
authors.initials: W
authors.lastname: Yuan
authors.forename: Matthew
authors.initials: M
authors.lastname: Stremlau
authors.forename: Claudia
authors.initials: C
authors.lastname: Mische
authors.forename: Hassan
authors.initials: H
authors.lastname: Javanbakht
authors.forename: Mark
authors.initials: M
authors.lastname: Scally
authors.forename: Cheryl
authors.initials: C
authors.lastname: Winkler
authors.forename: Michael
authors.initials: M
authors.lastname: Dean
authors.forename: Joseph
authors.initials: J
authors.lastname: Sodroski
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000378:metabolism; D000818:Animals; D000090103:Antiviral Restriction Factors; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D003593:Cytoplasm / Q000737:chemistry; D004285:Dogs; D015497:HIV-1 / Q000276:immunology / Q000502:physiology*; D006367:HeLa Cells; D006801:Humans; D008253:Macaca mulatta; D008565:Membrane Proteins / Q000378:metabolism; D019251:Nucleocapsid / Q000378:metabolism*; D010802:Phylogeny; D011485:Protein Binding; D000070584:Tripartite Motif Proteins; D044767:Ubiquitin-Protein Ligases
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D000090103:Antiviral Restriction Factors; D002352:Carrier Proteins; D008565:Membrane Proteins; C114030:TRAT1 protein, human; C417918:TRIM34 protein, human; D000070584:Tripartite Motif Proteins; C477346:TRIM5 protein, human; D044767:Ubiquitin-Protein Ligases