Linked Life Data

9151825

Source:http://linkedlifedata.com/resource/pubmed/id/9151825

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1997-6-9
pubmed:abstractText
Recently, we have shown that the ability of the flavivirus NS2B-NS3 protease complex to promote efficient signalase processing of the C-prM precursor, as well as secretion of prM and E, does not appear to depend strictly on cleavage of the precursor at its Lys-Arg-Gly dibasic site by the protease. We suggested that the association of the protease with the precursor via NS2B may be sufficient by itself for the above effects. To study the proposed association in more detail, we have developed an assay in which processing at the C-prM dibasic cleavage site is abolished by Lys-->Gly conversion. We constructed deletion mutants and chimeras of the West Nile (WN) flavivirus NS2B protein and expressed them in the context of [5'-C-->NS3(243)] containing either wild-type C-prM or its cleavage site mutant. All NS2B variants were able to form active protease complexes. Deletion of the carboxy-terminal cluster of hydrophobic amino acids in NS2B had no apparent effect on the formation of prM and prM-E secretion for the cassettes containing either wild-type or mutated C-prM precursor. Deletion of the amino-terminal hydrophobic cluster in NS2B did not affect prM-E secretion for the cassettes with wild-type C-prM but abrogated prM-E secretion for the cassettes with the mutated dibasic cleavage site in C-prM. Similarly, the NS2B-NS3(178) protease of Japanese encephalitis (JE) virus, when substituted for the WN virus NS2B-NS3(243) protease, was able to promote prM-E secretion for the cassette with the wild-type C-prM precursor but not with the mutated one. Replacement of the deleted amino-terminal hydrophobic cluster in the WN virus NS2B protein with an analogous JE virus sequence restored the ability of the protease to promote prM-E secretion. On the basis of these observations, roles of individual protease components in upregulation of C-prM signalase processing are discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-1826736, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-1833562, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-1845826, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2016768, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2147282, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2174669, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2353452, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2501515, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2522997, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2543956, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2546125, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2548336, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2674479, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2705302, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2741348, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2826667, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-2952760, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-3094962, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-3095828, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-3686827, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-3753811, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-5828097, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-7108955, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-7494334, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-7884844, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-7897348, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-7958993, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8057458, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8116234, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8189517, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8383225, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8392191, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8411382, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8460492, http://linkedlifedata.com/resource/pubmed/commentcorrection/9151825-8517028
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4364-71
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Upregulation of signalase processing and induction of prM-E secretion by the flavivirus NS2B-NS3 protease: roles of protease components.
pubmed:affiliation
Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't