Show simple item record Wagner, Jonathan M. Christensen, Devin E. Bhattacharya, Akash Dawidziak, Daria M. Roganowicz, Marcin D. Wan, Yueping Pumroy, Ruth A. Demeler, Borries Ivanov, Dmitri N. Ganser-Pornillos, Barbie K. Sundquist, Wesley I. Pornillos, Owen 2021-09-23T18:52:49Z 2021-09-23T18:52:49Z 2018
dc.identifier.citation Wagner, J. M., Christensen, D. E., Bhattacharya, A., Dawidziak, D. M., Roganowicz, M. D., Wan, Y., Pumroy, R. A., Demeler, B., Ivanov, D. N., Ganser-Pornillos, B. K., Sundquist, W. I., & Pornillow, O. (2018). General model for retroviral capsid pattern recognition by TRIM5 proteins. Journal of Virology, 92(4), Article e01563-17. en_US
dc.description Permission to archive final published version en_US
dc.description.abstract Restriction factors are intrinsic cellular defense proteins that have evolved to block microbial infections. Retroviruses such as HIV-1 are restricted by TRIM5 proteins, which recognize the viral capsid shell that surrounds, organizes, and protects the viral genome. TRIM5α uses a SPRY domain to bind capsids with low intrinsic affinity (KD of >1 mM) and therefore requires higher-order assembly into a hexagonal lattice to generate sufficient avidity for productive capsid recognition. TRIMCyp, on the other hand, binds HIV-1 capsids through a cyclophilin A domain, which has a well-defined binding site and higher affinity (KD of ∼10 μM) for isolated capsid subunits. Therefore, it has been argued that TRIMCyp proteins have dispensed with the need for higher-order assembly to function as antiviral factors. Here, we show that, consistent with its high degree of sequence similarity with TRIM5α, the TRIMCyp B-box 2 domain shares the same ability to self-associate and facilitate assembly of a TRIMCyp hexagonal lattice that can wrap about the HIV-1 capsid. We also show that under stringent experimental conditions, TRIMCyp-mediated restriction of HIV-1 is indeed dependent on higher-order assembly. Both forms of TRIM5 therefore use the same mechanism of avidity-driven capsid pattern recognition en_US
dc.language.iso en_US en_US
dc.publisher American Society for Microbiology en_US
dc.subject Pattern recognition en_US
dc.subject Restriction factor en_US
dc.subject Retrovirus en_US
dc.subject TRIM5 proteins
dc.subject.lcsh Pattern perception
dc.title General model for retroviral capsid pattern recognition by TRIM5 proteins en_US
dc.type Article en_US
dc.publisher.faculty Arts and Science en_US
dc.publisher.department Department of Chemistry and Biochemistry en_US
dc.description.peer-review Yes en_US
dc.publisher.institution University of Virginia en_US
dc.publisher.institution University of Utah en_US
dc.publisher.institution University of Texas Health Science Center at San Antonio en_US
dc.publisher.institution University of Lethbridge en_US
dc.publisher.url en_US

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