Key result
Human IgA monoclonal antibodies block norovirus VLP binding to host factors more effectively than IgG.
Human IgA monoclonal antibodies appear more potent than IgG antibodies in blocking norovirus binding to host attachment factors, highlighting a unique role for IgA in mucosal protection.
Noroviruses (NoV) are the most common cause of non-bacterial acute gastroenteritis and cause local outbreaks of illness, especially in confined situations. Despite being identified four decades ago, the correlates of protection against norovirus gastroenteritis are still being elucidated. Recent studies have shown an association of protection with NoV-specific serum histo-blood group antigen-blocking antibody and with serum IgA in patients vaccinated with NoV VLPs. Here, we describe the isolation and characterization of human monoclonal IgG and IgA antibodies against a GI.I NoV, Norwalk virus (NV). A higher proportion of the IgA antibodies blocked NV VLP binding to glycans than did IgG antibodies. We generated isotype-switched variants of IgG and IgA antibodies to study the effects of the constant domain on blocking and binding activities. The IgA form of antibodies appears to be more potent than the IgG form in blocking norovirus binding to histo-blood group antigens. These studies suggest a unique role for IgA antibodies in protection from NoV infections by blocking attachment to cell receptors.
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Sapparapu et al. (2016) studied Norovirus infection (n=2). IgA monoclonal antibodies vs. IgG monoclonal antibodies was evaluated on Blocking of norovirus VLP binding to histo-blood group antigens. Human IgA monoclonal antibodies blocked GI.1 norovirus virus-like particles from binding to synthetic host attachment factors more effectively than did IgG antibodies.
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