You are not logged in.

Alteration of the proline at position 7 of the HIV-1 spacer peptide p1 suppresses viral infectivity in a strain dependent manner

Hill, Melissa K., Bellamy-McIntyre, Anna, Vella, Laura J., Campbell, Shahan M., Marshall, John A., Tachedjian, Gilda and Mak, Johnson 2007, Alteration of the proline at position 7 of the HIV-1 spacer peptide p1 suppresses viral infectivity in a strain dependent manner, Current HIV research, vol. 5, no. 1, pp. 69-78.

Attached Files
Name Description MIMEType Size Downloads

Title Alteration of the proline at position 7 of the HIV-1 spacer peptide p1 suppresses viral infectivity in a strain dependent manner
Author(s) Hill, Melissa K.
Bellamy-McIntyre, Anna
Vella, Laura J.
Campbell, Shahan M.
Marshall, John A.
Tachedjian, Gilda
Mak, JohnsonORCID iD for Mak, Johnson orcid.org/0000-0002-5229-5707
Journal name Current HIV research
Volume number 5
Issue number 1
Start page 69
End page 78
Total pages 11
Publisher Bentham Science Publishers
Place of publication Bussum, Netherlands
Publication date 2007-01
ISSN 1570-162X
1873-4251
Keyword(s) HIV
spacer peptide
p1
p6Gag
Gag
Summary The HIV-1 spacer peptide p1 is located in the C-terminus of the Gag polyprotein and separates the nucleocapsid (NC) and p6(Gag). Research centered on p1 has been limited and as yet no function has been ascribed to this spacer peptide. We have previously found that the conserved p1 proline residues (position 7 and 13) are critical for replication in the HIV-1 strain HXB2-BH10. In this study we have focused on the proline rich p1-p6(Gag) C-terminus of HIV-1. We individually examined the role of p1 proline's in multiple strains of HIV-1 and investigated the role of three proline residues in p6(Gag) (P24, P25 and P30). Assessment of the HXB2-BH10 based mutants revealed that Gag-Pol incorporation relative to Gag decreased in the p1 mutant virions, with the double proline mutant the most impaired. Mutating both p1 proline residues was found to abolish infectivity in multiple strains of HIV-1. Independent mutation of the p1 proline at position 7 resulted in a strain-dependent suppression of viral infectivity. This defect correlates with the presence of a tyrosine residue at position 9 of p1 and occurs in the early phase of the HIV-1 replication cycle. The p1 proline residues were found to be functionally distinct from P24, P25 and P30 in p6(Gag). This work affords novel insights into our understanding of the role of p1 in HIV-1 replication.
Language eng
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2007, Bentham Science Publishers
Persistent URL http://hdl.handle.net/10536/DRO/DU:30047457

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

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 3 times in TR Web of Science
Scopus Citation Count Cited 3 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 251 Abstract Views, 2 File Downloads  -  Detailed Statistics
Created: Thu, 30 Aug 2012, 09:31:53 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.