Structure of the rhesus monkey TRIM5α PRYSPRY domain, the HIV capsid recognition module

被引:81
作者
Biris, Nikolaos [1 ]
Yang, Yang [3 ]
Taylor, Alexander B. [1 ]
Tomashevski, Andrei [1 ]
Guo, Miao [1 ]
Hart, P. John [1 ,4 ]
Diaz-Griffero, Felipe [3 ]
Ivanov, Dmitri N. [1 ,2 ]
机构
[1] Univ Texas Hlth Sci Ctr San Antonio, Dept Biochem, San Antonio, TX 78229 USA
[2] Univ Texas Hlth Sci Ctr San Antonio, Canc Therapy & Res Ctr, San Antonio, TX 78229 USA
[3] Albert Einstein Coll Med, Dept Microbiol & Immunol, Bronx, NY 10461 USA
[4] S Texas Vet Hlth Care Syst, Dept Vet Affairs, Geriatr Res Educ & Clin Ctr, San Antonio, TX 78229 USA
基金
美国国家卫生研究院;
关键词
RETROVIRAL RESTRICTION; B30.2(SPRY) DOMAIN; B30.2/SPRY DOMAIN; SPRY DOMAIN; PROTEINS; DETERMINANTS; EVOLUTION; INFECTION; POTENCY; BINDING;
D O I
10.1073/pnas.1203536109
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Tripartite motif protein TRIM5 alpha blocks retroviral replication after cell entry, and species-specific differences in its activity are determined by sequence variations within the C-terminal B30.2/PRYSPRY domain. Here we report a high-resolution structure of a TRIM5 alpha PRYSPRY domain, the PRYSPRY of the rhesus monkey TRIM5 alpha that potently restricts HIV infection, and identify features involved in its interaction with the HIV capsid. The extensive capsid-binding interface maps on the structurally divergent face of the protein formed by hypervariable loop segments, confirming that TRIM5 alpha evolution is largely determined by its binding specificity. Interactions with the capsid are mediated by flexible variable loops via a mechanism that parallels antigen recognition by IgM antibodies, a similarity that may help explain some of the unusual functional properties of TRIM5 alpha. Distinctive features of this pathogen-recognition interface, such as structural plasticity conferred by the mobile v1 segment and interaction with multiple epitopes, may allow restriction of divergent retroviruses and increase resistance to capsid mutations.
引用
收藏
页码:13278 / 13283
页数:6
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