Linked Life Data

15564494

Source:http://linkedlifedata.com/resource/pubmed/id/15564494

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2004-11-26
pubmed:abstractText
Analogous to cellular glycoproteins, viral envelope proteins contain N-terminal signal sequences responsible for targeting them to the secretory pathway. The prototype foamy virus (PFV) envelope (Env) shows a highly unusual biosynthesis. Its precursor protein has a type III membrane topology with both the N and C terminus located in the cytoplasm. Coexpression of FV glycoprotein and interaction of its leader peptide (LP) with the viral capsid is essential for viral particle budding and egress. Processing of PFV Env into the particle-associated LP, surface (SU), and transmembrane (TM) subunits occur posttranslationally during transport to the cell surface by yet-unidentified cellular proteases. Here we provide strong evidence that furin itself or a furin-like protease and not the signal peptidase complex is responsible for both processing events. N-terminal protein sequencing of the SU and TM subunits of purified PFV Env-immunoglobulin G immunoadhesin identified furin consensus sequences upstream of both cleavage sites. Mutagenesis analysis of two overlapping furin consensus sequences at the PFV LP/SU cleavage site in the wild-type protein confirmed the sequencing data and demonstrated utilization of only the first site. Fully processed SU was almost completely absent in viral particles of mutants having conserved arginine residues replaced by alanines in the first furin consensus sequence, but normal processing was observed upon mutation of the second motif. Although these mutants displayed a significant loss in infectivity as a result of reduced particle release, no correlation to processing inhibition was observed, since another mutant having normal LP/SU processing had a similar defect.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-10074106, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-10684317, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-10775583, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-11063880, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-11390578, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-11483744, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-11520859, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-11714958, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-12360192, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-12781711, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-12908766, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-12908770, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-3031469, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-4132053, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-8091657, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-8394455, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-9151877, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-9557698, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-9789330, http://linkedlifedata.com/resource/pubmed/commentcorrection/15564494-9934708
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
13865-70
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Prototype foamy virus envelope glycoprotein leader peptide processing is mediated by a furin-like cellular protease, but cleavage is not essential for viral infectivity.
pubmed:affiliation
Institut für Virologie, Medizinische Fakultät Carl Gustav Carus, Technische Universität Dresden, Fetscherstr. 74, 01307 Dresden, Germany. dirk.lindemann@mailbox.tu-dresden.de.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't