General model for retroviral capsid pattern recognition by TRIM5 proteins

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dc.contributor.authorWagner, Jonathan M.
dc.contributor.authorChristensen, Devin E.
dc.contributor.authorBhattacharya, Akash
dc.contributor.authorDawidziak, Daria M.
dc.contributor.authorRoganowicz, Marcin D.
dc.contributor.authorWan, Yueping
dc.contributor.authorPumroy, Ruth A.
dc.contributor.authorDemeler, Borries
dc.contributor.authorIvanov, Dmitri N.
dc.contributor.authorGanser-Pornillos, Barbie K.
dc.contributor.authorSundquist, Wesley I.
dc.contributor.authorPornillos, Owen
dc.date.accessioned2021-09-23T18:52:49Z
dc.date.available2021-09-23T18:52:49Z
dc.date.issued2018
dc.descriptionPermission to archive final published versionen_US
dc.description.abstractRestriction 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 recognitionen_US
dc.description.peer-reviewYesen_US
dc.identifier.citationWagner, 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.01563-17en_US
dc.identifier.urihttps://hdl.handle.net/10133/6040
dc.language.isoen_USen_US
dc.publisherAmerican Society for Microbiologyen_US
dc.publisher.departmentDepartment of Chemistry and Biochemistryen_US
dc.publisher.facultyArts and Scienceen_US
dc.publisher.institutionUniversity of Virginiaen_US
dc.publisher.institutionUniversity of Utahen_US
dc.publisher.institutionUniversity of Texas Health Science Center at San Antonioen_US
dc.publisher.institutionUniversity of Lethbridgeen_US
dc.publisher.urlhttps://doi.org/10.1128/JVI.01563-17en_US
dc.subjectPattern recognitionen_US
dc.subjectRestriction factoren_US
dc.subjectRetrovirusen_US
dc.subjectTRIM5 proteins
dc.subject.lcshPattern perception
dc.titleGeneral model for retroviral capsid pattern recognition by TRIM5 proteinsen_US
dc.typeArticleen_US
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