dc.contributor.author |
Goldstone, David |
en |
dc.contributor.author |
Yap, Melvyn W |
en |
dc.contributor.author |
Robertson, Laura E |
en |
dc.contributor.author |
Haire, Lesley F |
en |
dc.contributor.author |
Taylor, William R |
en |
dc.contributor.author |
Katzourakis, Aris |
en |
dc.contributor.author |
Stoye, Jonathan P |
en |
dc.contributor.author |
Taylor, Ian A |
en |
dc.date.accessioned |
2012-05-13T21:23:39Z |
en |
dc.date.issued |
2010-09-16 |
en |
dc.identifier.citation |
Cell Host and Microbe 8(3):248-259 16 Sep 2010 |
en |
dc.identifier.issn |
1931-3128 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/17929 |
en |
dc.description.abstract |
Lentiviruses are widespread in a variety of vertebrates, often associated with chronic disease states. However, until the recent discovery of the prehistoric endogenous lentiviruses in rabbits (RELIK) and lemurs (PSIV), it was thought that lentiviruses had no capacity for germline integration and were only spread horizontally in an exogenous fashion. The existence of RELIK and PSIV refuted these ideas, revealing lentiviruses to be present in a range of mammals, capable of germline integration, and far more ancient than previously thought. Using Gag sequences reconstructed from the remnants of these prehistoric lentiviruses, we have produced chimeric lentiviruses capable of infecting nondividing cells and determined structures of capsid domains from PSIV and RELIK. We show that the structures from these diverse viruses are highly similar, containing features found in modern-day lentiviruses, including a functional cyclophilin-binding loop. Together, these data provide evidence for an ancient capsid-cyclophilin interaction preserved throughout lentiviral evolution. |
en |
dc.language |
English |
en |
dc.publisher |
Elsevier (Cell Press) |
en |
dc.relation.ispartofseries |
Cell Host and Microbe |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1931-3128/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Science & Technology |
en |
dc.subject |
Life Sciences & Biomedicine |
en |
dc.subject |
Microbiology |
en |
dc.subject |
Parasitology |
en |
dc.subject |
Virology |
en |
dc.subject |
IMMUNODEFICIENCY-VIRUS TYPE-1 |
en |
dc.subject |
AMINO-TERMINAL DOMAIN |
en |
dc.subject |
CYCLOPHILIN-A |
en |
dc.subject |
TRIM5-ALPHA RESTRICTION |
en |
dc.subject |
REVERSE TRANSCRIPTION |
en |
dc.subject |
ENDOGENOUS LENTIVIRUS |
en |
dc.subject |
CRYSTAL-STRUCTURE |
en |
dc.subject |
CYCLOSPORINE-A |
en |
dc.subject |
HIV-1 VIRIONS |
en |
dc.subject |
LIFE-CYCLE |
en |
dc.title |
Structural and Functional Analysis of Prehistoric Lentiviruses Uncovers an Ancient Molecular Interface |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1016/j.chom.2010.08.006 |
en |
pubs.issue |
3 |
en |
pubs.begin-page |
248 |
en |
pubs.volume |
8 |
en |
dc.rights.holder |
Copyright: Elsevier (Cell Press) |
en |
dc.identifier.pmid |
20833376 |
en |
pubs.author-url |
http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000282626900006&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=6e41486220adb198d0efde5a3b153e7d |
en |
pubs.end-page |
259 |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
285411 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.record-created-at-source-date |
2012-05-14 |
en |
pubs.dimensions-id |
20833376 |
en |