6533b7ddfe1ef96bd1273e73

RESEARCH PRODUCT

Inhibition of human immunodeficiency virus-1 infection by human conglutinin-like protein: in vitro studies.

Miroslav J. GašićHiroshi UshijimaEckart MatthesSlobodan PoznanovicWerner E.g. MüllerHeinz C. Schröder

subject

Cancer ResearchMolecular Sequence DataCarbohydratesImmunoglobulinsEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp120Mannose-Binding LectinVirusChromatography AffinityArticleViral ProteinsConglutininProtein A/GHumansImmunoconglutininsBinding siteKey wordsConglutinin‐like proteinchemistry.chemical_classificationAcquired Immunodeficiency SyndromebiologyHIV‐1Immunization PassiveLectinMolecular biologyMannanIn vitrogp120OncologychemistryCarbohydrate Sequencebiology.proteinHIV-1Protein GGlycoproteinCarrier ProteinsLectin

description

The lectin-like protein analogous to bovine conglutinin was purified from human serum. The carbohydrate-binding ability of conglutinin-like protein was inhibited by D-mannose, N-acetylglucosamine and L-fucose as well as by mannan-containing oligosaccharides. By applying a lectin-based ELISA system it was demonstrated that conglutinin-like protein binds to human immunodeficiency virus-1 (HIV-1) glycoprotein 120 (gp120) via its carbohydrate binding site. In vitro experiments with T-lymphoblastoid CEM cells revealed that conglutinin-like protein abolishes infection by HIV-1; a 50% cytoprotective concentration of 23.9 micrograms/ml was measured. These findings demonstrate that human conglutinin-like protein binds to HIV-gp120 and inhibits, under the described in vitro conditions, CEM cell infection.

10.1111/j.1349-7006.1992.tb01950.xhttps://pubmed.ncbi.nlm.nih.gov/1618696