You are not logged in.
Openly accessible

The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV

Tanwar, Hanumantsingh, Khoo, Keith K., Garvey, Megan, Waddington, Lynne, Leis, Andrew, Hijnen, Marcel, Velkov, Tony, Dumsday, Geoff J., McKinstry, William J. and Mak, Johnson 2017, The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV, PLoS pathogens, vol. 13, no. 2, pp. 1-24, doi: 10.0.5.91/journal.ppat.1006221.

Attached Files
Name Description MIMEType Size Downloads
tanwar-thermodynamics-2017.pdf Published version application/pdf 2.48MB 1

Title The thermodynamics of Pr55Gag-RNA interaction regulate the assembly of HIV
Author(s) Tanwar, Hanumantsingh
Khoo, Keith K.
Garvey, Megan
Waddington, Lynne
Leis, Andrew
Hijnen, Marcel
Velkov, Tony
Dumsday, Geoff J.
McKinstry, William J.
Mak, JohnsonORCID iD for Mak, Johnson orcid.org/0000-0002-5229-5707
Journal name PLoS pathogens
Volume number 13
Issue number 2
Article ID e1006221
Start page 1
End page 24
Total pages 24
Publisher Public Library of Science
Place of publication San Francisco, Calif.
Publication date 2017-02-21
ISSN 1553-7366
Summary The interactions that occur during HIV Pr55Gag oligomerization and genomic RNA packagingare essential elements that facilitate HIV assembly. However, mechanistic details ofthese interactions are not clearly defined. Here, we overcome previous limitations in producinglarge quantities of full-length recombinant Pr55Gag that is required for isothermal titrationcalorimetry (ITC) studies, and we have revealed the thermodynamic properties of HIVassembly for the first time. Thermodynamic analysis showed that the binding between RNAand HIV Pr55Gag is an energetically favourable reaction (ΔG<0) that is further enhanced bythe 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 stepwiseincrements of heat being released during HIV biogenesis may help to facilitate the processof viral assembly. By mimicking the interactions between A-containing RNA and oligomericPr55Gag in immature HIV, it was noted that a p6 domain truncated Pr50Gag Δp6 is less efficientthan full-length Pr55Gag in this thermodynamic process. These data suggest a potentialunknown role of p6 in Pr55Gag-Pr55Gag oligomerization and/or Pr55Gag-RNA interaction duringHIV assembly. Our data provide direct evidence on how nucleic acid sequences and theoligomeric state of Pr55Gag regulate HIV assembly.
Language eng
DOI 10.0.5.91/journal.ppat.1006221
Field of Research 110804 Medical Virology
110802 Medical Infection Agents (incl Prions)
0605 Microbiology
1107 Immunology
1108 Medical Microbiology
Socio Economic Objective 920109 Infectious Diseases
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2017, The Authors
Free to Read? Yes
Use Rights Creative Commons Attribution licence
Persistent URL http://hdl.handle.net/10536/DRO/DU:30091566

Document type: Journal Article
Collections: School of Medicine
Open Access Collection
Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 0 times in TR Web of Science
Scopus Citation Count Cited 0 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 7 Abstract Views, 2 File Downloads  -  Detailed Statistics
Created: Fri, 24 Mar 2017, 15:16:40 EST

Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.