Journal article

THE STOICHIOMETRY OF BINDING BETWEEN MONOCLONAL-ANTIBODY MOLECULES AND THE HEMAGGLUTININ OF INFLUENZA-VIRUS

P POUMBOURIOS, LE BROWN, DO WHITE, DC JACKSON

VIROLOGY | ACADEMIC PRESS INC ELSEVIER SCIENCE | Published : 1990

Abstract

The number of neutralizing monoclonal IgG molecules that can bind to a single trimeric molecule of influenza viral hemagglutinin (HA) was calculated by estimating the molecular weight of the immune complexes formed under conditions of antibody excess and was found to be dependent upon the antigenic site to which the MAb is directed. Whereas three antibody molecules directed to site A or site E are able to bind simultaneously to a single trimer of HA, generally only one molecule directed to site B (the "tip") or site B/D ("tip/interface") can be accommodated. Using mixtures of MAbs, more IgG molecules can be accommodated, but steric hindrance limits simultaneous binding of different MAbs dire..

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