Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-4-15
pubmed:abstractText
The functional roles of the matrix (MA) protein in the assembly and maturation of retroviruses was investigated with a series of MA mutants of Mason-Pfizer monkey virus (M-PMV), an immunosuppressive type D retrovirus. The mutants we describe here were generated by the introduction of random point mutations within the MA coding domain by use of sodium bisulphite mutagenesis. Studies of these mutants show that the MA protein plays a critical role in three different, sequential events in the final stages of type D retrovirus replication: (i) folding of the gag gene-encoded precursor poly-proteins into a stable conformation for capsid assembly in the cytoplasm of infected cells; (ii) capsid transport from the site of assembly to the plasma membrane; and (iii) capsid association with, and extrusion of the membrane during virus budding. The mutants described here interfere with or block M-PMV replication at each of these stages. Large numbers of preassembled capsids accumulate within the cytoplasm of transport-defective mutant-infected cells, suggesting that transport of M-PMV capsids to the plasma membrane is an active and specific intracellular targeting process. The initial association of the capsid with the membrane may depend upon this intracytoplasmic transport process but additional protein-lipid interactions that involve the MA protein are required for membrane extrusion around the preformed capsids; in cells infected with the budding-defective mutant, assembled capsids accumulate under the inner surface of the cell plasma membrane, and are retarded in their release from the infected cell.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-10793721, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-187721, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-202022, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-205999, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-208256, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-209457, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2170021, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-217152, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2200887, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-229234, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2370682, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2421920, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2535744, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2578615, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2649693, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-271968, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2788277, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2825164, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2993920, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2994218, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-2997984, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3052287, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3083581, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3292789, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3485855, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3489936, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3493352, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3643678, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3670292, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-3927012, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-4288418, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-4357873, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-4705382, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-4736082, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6094591, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6096101, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6255212, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6302307, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6329679, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6333757, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6340098, http://linkedlifedata.com/resource/pubmed/commentcorrection/1705884-6608821
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0261-4189
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
535-46
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Amino acid substitutions within the matrix protein of type D retroviruses affect assembly, transport and membrane association of a capsid.
pubmed:affiliation
Department of Microbiology, University of Alabama, Birmingham 35294.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.