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dc.contributor.authorTanwar, Hanumant S
dc.contributor.authorKhoo, Keith K
dc.contributor.authorGarvey, Megan
dc.contributor.authorWaddington, Lynne
dc.contributor.authorLeis, Andrew
dc.contributor.authorHijnen, Marcel
dc.contributor.authorVelkov, Tony
dc.contributor.authorDumsday, Geoff J
dc.contributor.authorMcKinstry, William J
dc.contributor.authorMak, Johnson
dc.date.accessioned2021-10-28T04:14:20Z
dc.date.available2021-10-28T04:14:20Z
dc.date.issued2017
dc.identifier.issn1553-7366
dc.identifier.doi10.1371/journal.ppat.1006221
dc.identifier.urihttp://hdl.handle.net/10072/409519
dc.description.abstractThe interactions that occur during HIV Pr55Gagoligomerization and genomic RNA packaging are essential elements that facilitate HIV assembly. However, mechanistic details of these interactions are not clearly defined. Here, we overcome previous limitations in producing large quantities of full-length recombinant Pr55Gagthat is required for isothermal titration calorimetry (ITC) studies, and we have revealed the thermodynamic properties of HIV assembly for the first time. Thermodynamic analysis showed that the binding between RNA and HIV Pr55Gagis an energetically favourable reaction (ΔG<0) that is further enhanced by the oligomerization of Pr55Gag. The change in enthalpy (ΔH) widens sequentially from: (1) Pr55Gag-Psi RNA binding during HIV genome selection; to (2) Pr55Gag-Guanosine Uridine (GU)-containing RNA binding in cytoplasm/plasma membrane; and then to (3) Pr55Gag-Adenosine(A)-containing RNA binding in immature HIV. These data imply the stepwise increments of heat being released during HIV biogenesis may help to facilitate the process of viral assembly. By mimicking the interactions between A-containing RNA and oligomeric Pr55Gagin immature HIV, it was noted that a p6 domain truncated Pr50Gag Δp6is less efficient than full-length Pr55Gagin this thermodynamic process. These data suggest a potential unknown role of p6 in Pr55Gag-Pr55Gagoligomerization and/or Pr55Gag-RNA interaction during HIV assembly. Our data provide direct evidence on how nucleic acid sequences and the oligomeric state of Pr55Gagregulate HIV assembly.
dc.description.peerreviewedYes
dc.languageEnglish
dc.publisherPUBLIC LIBRARY SCIENCE
dc.relation.ispartofjournalPLOS Pathogens
dc.relation.ispartofvolume13
dc.subject.fieldofresearchMicrobiology
dc.subject.fieldofresearchImmunology
dc.subject.fieldofresearchMedical microbiology
dc.subject.fieldofresearchcode3107
dc.subject.fieldofresearchcode3204
dc.subject.fieldofresearchcode3207
dc.subject.keywordsScience & Technology
dc.subject.keywordsLife Sciences & Biomedicine
dc.subject.keywordsMicrobiology
dc.subject.keywordsParasitology
dc.subject.keywordsVirology
dc.titleThe thermodynamics of Pr55(Gag)-RNA interaction regulate the assembly of HIV
dc.typeJournal article
dc.type.descriptionC1 - Articles
dcterms.bibliographicCitationTanwar, HS; Khoo, KK; Garvey, M; Waddington, L; Leis, A; Hijnen, M; Velkov, T; Dumsday, GJ; McKinstry, WJ; Mak, J, The thermodynamics of Pr55(Gag)-RNA interaction regulate the assembly of HIV, PLOS Pathogens, 2017, 13
dcterms.dateAccepted2017-02-06
dc.date.updated2021-10-28T04:13:10Z
gro.hasfulltextNo Full Text
gro.griffith.authorMak, Johnson


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