Linked Life Data

9764911

Source:http://linkedlifedata.com/resource/pubmed/id/9764911

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1998-12-17
pubmed:databankReference
pubmed:abstractText
The immunoreactivity, functional activity, and molecular features of a human monoclonal antibody (HMAb), F240, from an HIV-1-infected individual have been studied. Flow cytometric analysis demonstrated that F240 is reactive with cells infected with a broad range of laboratory isolates but not with uninfected cells. Reactivity of F240 is greatly enhanced by preincubation of infected cells with soluble CD4, and to a much lesser extent, with F105, an HMAb reactive with the CD4-binding site of gp120. This enhancement is temperature dependent, with maximum enhancement observed at 37 degrees C, and suggests that the F240 epitope may be more accessible after gp120 has bound to CD4 in vivo. Immunoblot analysis reveals antigen specificity of F240 for gp41 or its precursor gp160. F240 specificity is mapped to the immunodominant region of the gp41 ectodomain by Pepscan analysis. This epitope has been implicated in eliciting nonprotective antibodies that enhance infection in the presence of complement. Consistent with this, F240 failed to neutralize laboratory isolates and enhanced viral infection in a complement-dependent manner. The F240 VH demonstrates extensive somatic mutations compared with the product of its closest homologous germline gene VH3-3.11. Most amino acid substitutions occur in CDR2, characteristic of an antigen-driven response, and in FR3, a phenomenon observed in other anti-HIV-1 envelope HMAbs. Primary structure analysis of the F240 heavy chain revealed strong homology in the CDR domains to an HMAb (3D6) reactive with the same gp41 region, which suggests that these HMAbs could define a potential human antibody clonotype.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0889-2229
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1271-80
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9764911-Amino Acid Sequence, pubmed-meshheading:9764911-Animals, pubmed-meshheading:9764911-Antibodies, Monoclonal, pubmed-meshheading:9764911-Blotting, Western, pubmed-meshheading:9764911-Cloning, Molecular, pubmed-meshheading:9764911-Complement System Proteins, pubmed-meshheading:9764911-Genes, Immunoglobulin, pubmed-meshheading:9764911-HIV Envelope Protein gp120, pubmed-meshheading:9764911-HIV Envelope Protein gp41, pubmed-meshheading:9764911-HIV Infections, pubmed-meshheading:9764911-HIV-1, pubmed-meshheading:9764911-Humans, pubmed-meshheading:9764911-Immunodominant Epitopes, pubmed-meshheading:9764911-Immunoglobulin Heavy Chains, pubmed-meshheading:9764911-Immunoglobulin Light Chains, pubmed-meshheading:9764911-Mice, pubmed-meshheading:9764911-Molecular Sequence Data, pubmed-meshheading:9764911-Sequence Analysis, DNA
pubmed:year
1998
pubmed:articleTitle
Functional and molecular characterization of human monoclonal antibody reactive with the immunodominant region of HIV type 1 glycoprotein 41.
pubmed:affiliation
Department of Medicine, Beth Israel Deaconess Medical Center and Harvard Medical School, Boston, Massachusetts 02215, USA. lcavacin@bidmc.harvard.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.