Potential Role of Nonneutralizing IgA Antibodies in Cross-Protective Immunity against Influenza A Viruses of Multiple Hemagglutinin Subtypes.
Animals
Antibodies, Monoclonal
/ genetics
Antibodies, Neutralizing
/ genetics
Antibodies, Viral
/ genetics
Cross Protection
Cross Reactions
Dogs
Female
HEK293 Cells
Hemagglutinin Glycoproteins, Influenza Virus
/ classification
Humans
Immunity, Mucosal
Immunoglobulin A
/ genetics
Immunoglobulin G
/ genetics
Influenza A Virus, H1N1 Subtype
/ genetics
Influenza A Virus, H2N2 Subtype
/ genetics
Influenza A Virus, H5N1 Subtype
/ genetics
Influenza A virus
/ classification
Influenza, Human
/ immunology
Madin Darby Canine Kidney Cells
Mice
Mice, Inbred BALB C
Neutralization Tests
Orthomyxoviridae Infections
/ immunology
Virus Release
IgA
antibody
broadly cross-reactive
budding
cross-protective immunity
hemagglutinin
influenza A virus
nonneutralizing
Journal
Journal of virology
ISSN: 1098-5514
Titre abrégé: J Virol
Pays: United States
ID NLM: 0113724
Informations de publication
Date de publication:
01 06 2020
01 06 2020
Historique:
received:
07
03
2020
accepted:
28
03
2020
pubmed:
10
4
2020
medline:
20
11
2020
entrez:
10
4
2020
Statut:
epublish
Résumé
IgA antibodies on mucosal surfaces are known to play an important role in protection from influenza A virus (IAV) infection and are believed to be more potent than IgG for cross-protective immunity against IAVs of multiple hemagglutinin (HA) subtypes. However, in general, neutralizing antibodies specific to HA are principally HA subtype specific. Here, we focus on nonneutralizing but broadly cross-reactive HA-specific IgA antibodies. Recombinant IgG, monomeric IgA (mIgA), and polymeric secretory IgA (pSIgA) antibodies were generated based on the sequence of a mouse anti-HA monoclonal antibody (MAb) 5A5 that had no neutralizing activity but showed broad binding capacity to multiple HA subtypes. While confirming that there was no neutralizing activity of the recombinant MAbs against IAV strains A/Puerto Rico/8/1934 (H1N1), A/Adachi/2/1957 (H2N2), A/Hong Kong/483/1997 (H5N1), A/shearwater/South Australia/1/1972 (H6N5), A/duck/England/1/1956 (H11N6), and A/duck/Alberta/60/1976 (H12N5), we found that pSIgA, but not mIgA and IgG, significantly reduced budding and release of most of the viruses from infected cells. Electron microscopy demonstrated that pSIgA deposited newly produced virus particles on the surfaces of infected cells, most likely due to tethering of virus particles. Furthermore, we found that pSIgA showed significantly higher activity to reduce plaque sizes of the viruses than IgG and mIgA. These results suggest that nonneutralizing pSIgA reactive to multiple HA subtypes may play a role in intersubtype cross-protective immunity against IAVs.
Identifiants
pubmed: 32269119
pii: JVI.00408-20
doi: 10.1128/JVI.00408-20
pmc: PMC7307104
pii:
doi:
Substances chimiques
Antibodies, Monoclonal
0
Antibodies, Neutralizing
0
Antibodies, Viral
0
Hemagglutinin Glycoproteins, Influenza Virus
0
Immunoglobulin A
0
Immunoglobulin G
0
polymeric IgA
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2020 American Society for Microbiology.
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