Linked Life Data

7506556

Source:http://linkedlifedata.com/resource/pubmed/id/7506556

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1994-2-14
pubmed:abstractText
A human monoclonal antibody (HuMAb), 5145A, against HIV-1 gp120 was isolated from an asymptomatic, seropositive hemophiliac. The epitope of this HuMAb was destroyed by reduction of gp120 disulfide bonds, but not by removal of N-linked carbohydrates. This epitope overlaps the CD4-binding site of gp120, because binding of 5145A to gp120 is inhibited by soluble CD4 and by 1125H, a previously described HuMAb directed toward the CD4-binding site. However, the 5145A epitope differs from those of 1125H and other anti-CD4-binding site HuMAbs previously described, as documented by the viral strain specificity of 5145A and its reactivity with a panel of gp120 mutants. Specifically, 5145A reacted with 14 of 15 HIV-1 isolates tested, including 9 isolates from the Central African Republic, 6 of which were not recognized by 1125H. Partial epitope mapping of 5145A, using a series of gp120 mutants, demonstrated its lack of sensitivity to mutations in residues 257 and 427, contrasting with a marked sensitivity to mutations in residues 368 and 370. This pattern of reactivity distinguishes its epitope from that of any HuMAb against the CD4-binding site region described to date. In addition, 5145A exhibited potent and essentially equivalent neutralization of the MN, SF-2, IIIB, and RF strains and possessed significant neutralizing activity against three of three African strains tested. Finally, 5145A synergistically neutralized the MN and SF-2 strains of HIV-1 when combined with 4117C, a HuMAb against the V3 loop. The broad strain specificity and potent neutralizing activity of 5145A, together with its ability to synergize with an anti-V3 loop HuMAb in neutralizing HIV-1, indicate that 5145A has excellent potential as a passive immunotherapeutic agent against HIV-1.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0889-2229
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
985-96
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:7506556-Acquired Immunodeficiency Syndrome, pubmed-meshheading:7506556-Antibodies, Monoclonal, pubmed-meshheading:7506556-Antigens, CD4, pubmed-meshheading:7506556-Binding, Competitive, pubmed-meshheading:7506556-Binding Sites, Antibody, pubmed-meshheading:7506556-Blotting, Western, pubmed-meshheading:7506556-Central African Republic, pubmed-meshheading:7506556-Cross Reactions, pubmed-meshheading:7506556-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:7506556-Epitopes, pubmed-meshheading:7506556-Gene Products, env, pubmed-meshheading:7506556-HIV Antibodies, pubmed-meshheading:7506556-HIV Envelope Protein gp120, pubmed-meshheading:7506556-HIV-1, pubmed-meshheading:7506556-Humans, pubmed-meshheading:7506556-Neutralization Tests, pubmed-meshheading:7506556-North America
pubmed:year
1993
pubmed:articleTitle
A potent, neutralizing human monoclonal antibody against a unique epitope overlapping the CD4-binding site of HIV-1 gp120 that is broadly conserved across North American and African virus isolates.
pubmed:affiliation
Public Health Research Institute, New York, New York 10016.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't