Linked Life Data

9875331

Source:http://linkedlifedata.com/resource/pubmed/id/9875331

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-1-20
pubmed:abstractText
The ability to rearrange membranes is a unique feature of nonstructural proteins 2B, 2C, and 2BC of some picornaviruses. To analyze in detail membrane binding of the respective proteins of hepatitis A virus (HAV), they were transiently expressed in the vaccinia/T7 system, and their effect on membrane permeability was studied using beta-galactosidase as reporter. Although 2C had no effect, the significantly increased reporter activity observed in the extracellular space of 2B- and 2BC-expressing cells points to a specific effect of HAV proteins 2B and 2BC on membrane permeability. In biochemical fractionation studies, HAV 2C and 2BC showed properties of intregral membrane proteins, whereas 2B was associated with membranes as a peripheral protein. Proteinase 3C-mediated cleavage of precursor 2BC in vivo was most efficient when the enzyme was coexpressed in its precursor forms P3 or 3ABC, which both include the membrane-anchoring domain 3A. 3ABC showed the same solubility pattern as 2BC, suggesting that colocalization of 2BC and 3ABC might be required for the efficient liberation of 2B and 2C and occurs on membranes that have been proposed as the site of viral RNA replication.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
252
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
218-27
pubmed:dateRevised
2007-10-11
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Membrane permeability induced by hepatitis A virus proteins 2B and 2BC and proteolytic processing of HAV 2BC.
pubmed:affiliation
Institute for Medical Microbiology and Hygiene, Medical University of Lübeck, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't