Functional interplay between the B-box 2 and the B30.2(SPRY) domains of TRIM5 alpha

摘要

The retroviral restriction factors, TRIM5 alpha and TRIMCyp, consist of RING and 13-box 2 domains separated by a coiled coil from carboxyterminal domains. These carboxy-terminal domains (the B30.2(SPRY) domain in TRIM alpha(x and the cyclophilin A domain in TRIMCyp) recognize the retroviral capsid. Here we show that some B-box 2 changes in TRIM5 alpha(y, but not in TRIMCyp, resulted in decreased human immunodeficiency virus (HIV-1) capsid binding. The phenotypic effects of these 13-box 2 changes on the restriction of retroviral infection depended on the potency of restriction and the affinity of the TRIM5a interaction with the viral capsid, two properties specified by the B30.2(SPRY) domain. Thus, some alterations in the TRIM5 alpha 13-box 2 domain apparently affect the orientation or conformation of the B30.2(SPRY) domain, influencing capsid recognition. (C) 2007 Elsevier Inc. All rights reserved.