Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2004-6-8
pubmed:abstractText
Previous works have indicated that incorporation of surface glycoprotein into retroviruses such as the human immunodeficiency virus type 1 (HIV-1) is not a highly specific process because several cellular glycoproteins can be inserted within the mature viral particle. The mechanism(s) that govern the acquisition of such host constituents have remained so far elusive. In this study, we have investigated the role played by the viral envelope (Env) of HIV-1 in the acquisition of host intercellular adhesion molecule type I (ICAM-1). ICAM-1 proteins were still present on viruses carrying much lower levels of gp120/gp41 due to a mutation in the matrix (MA) domain or on Env-deficient viruses when produced in immortalized and primary human cell lines. Interestingly, infectivity of an HIV-1 MA mutant that carry a suboptimal amount of Env proteins was restored to a certain degree by the presence of ICAM-1 when infection was performed in cells expressing an activated form of its natural counter-ligand, LFA-1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
324
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
165-72
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Envelope glycoproteins are not required for insertion of host ICAM-1 into human immunodeficiency virus type 1 and ICAM-1-bearing viruses are still infectious despite a suboptimal level of trimeric envelope proteins.
pubmed:affiliation
Research Center in Infectious Diseases, CHUL Research Center, and Faculty of Medicine, Laval University, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't