Show simple item record

dc.contributor.author Wagner, Jonathan M.
dc.contributor.author Christensen, Devin E.
dc.contributor.author Bhattacharya, Akash
dc.contributor.author Dawidziak, Daria M.
dc.contributor.author Roganowicz, Marcin D.
dc.contributor.author Wan, Yueping
dc.contributor.author Pumroy, Ruth A.
dc.contributor.author Demeler, Borries
dc.contributor.author Ivanov, Dmitri N.
dc.contributor.author Ganser-Pornillos, Barbie K.
dc.contributor.author Sundquist, Wesley I.
dc.contributor.author Pornillos, Owen
dc.date.accessioned 2021-09-23T18:52:49Z
dc.date.available 2021-09-23T18:52:49Z
dc.date.issued 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. https://doi.org/10.1128/JVI.01563-17 en_US
dc.identifier.uri https://hdl.handle.net/10133/6040
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 https://doi.org/10.1128/JVI.01563-17 en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record