Abstract：
:Immunogenicity of inactivated virus or subviral vaccines may be enhanced by complexing with an IgG antibody. Such antibody would increase the uptake, processing and presentation of the vaccine's antigens by antigen presenting cells (APC), via the adhesion of the antibody-vaccine complex to Fc-receptors on macrophages and other APC. A natural antibody in humans, which may be generally exploited for this purpose, is the natural anti-Gal antibody. This antibody is ubiquitously produced as 1% of circulating IgG in humans and Old World primates, and it interacts specifically with the carbohydrate epitope Gal alpha 1-3 Gal beta 1-4 GlcNAc-R (termed the alpha-galactosyl epitope). This epitope is synthesized in large amounts in cells of nonprimate mammals and New World monkeys by the glycosylation enzyme alpha 1,3 galactosyltransferase. Here we describe in vitro studies on the ability of anti-Gal to bind to alpha-galactosyl epitopes on influenza virus propagated in mammalian cells, and to enhance presentation by APC of viral hemagglutinin antigenic determinants to specific helper T cell clones. The various approaches for achieving alpha-galactosyl epitope expression on virion and subviral vaccines are discussed.
journal_name
Vaccinejournal_title
Vaccineauthors
Galili U,Repik PM,Anaraki F,Mozdzanowska K,Washko G,Gerhard Wdoi
10.1016/0264-410x(95)00189-8subject
Has Abstractpub_date
1996-03-01 00:00:00pages
321-8issue
4eissn
0264-410Xissn
1873-2518pii
0264410X95001898journal_volume
14pub_type
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