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.
Skip Nav Destination
Article navigation
1 January 1985
Article|
January 01 1985
Mechanism of neutralization of influenza virus by secretory IgA is different from that of monomeric IgA or IgG.
H P Taylor
N J Dimmock
Online ISSN: 1540-9538
Print ISSN: 0022-1007
J Exp Med (1985) 161 (1): 198–209.
Citation
H P Taylor, N J Dimmock; Mechanism of neutralization of influenza virus by secretory IgA is different from that of monomeric IgA or IgG.. J Exp Med 1 January 1985; 161 (1): 198–209. doi: https://doi.org/10.1084/jem.161.1.198
Download citation file:
Sign in
Don't already have an account? Register
Client Account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Sign in via your Institution
Sign in via your InstitutionEmail alerts
Advertisement