Mechanism of neutralization of influenza virus by secretory IgA is different from that of monomeric IgA or IgG.

We have found that bile is a useful source of secretory IgA (scIgA) which can specifically neutralize influenza virus infectivity. Using purified scIgA, we compared the mechanism of neutralization with that mediated by IgA monomers (prepared from scIgA by differential reduction) and IgG. At 4 degrees C, scIgA prevented the attachment of neutralized virus, while neither monomeric IgA nor IgG had any affect on this process or on the subsequent stages of infection by which virion RNA accumulates in nuclei. At 25 and 37 degrees C, scIgA permitted the attachment of approximately half the neutralized virus, but the virus was not internalized. Clearly, the neutralization depends on the character of the antibody used. scIgA may act by steric hindrance (with attachment or penetration, depending on temperature), whereas IgA and IgG neutralize infectivity at a stage subsequent to accumulation of the virus genome in the nucleus.