Immunoglobulin A antibody composition is sculpted to bind the self gut microbiome.
Journal
Science immunology
ISSN: 2470-9468
Titre abrégé: Sci Immunol
Pays: United States
ID NLM: 101688624
Informations de publication
Date de publication:
15 07 2022
15 07 2022
Historique:
entrez:
20
7
2022
pubmed:
21
7
2022
medline:
23
7
2022
Statut:
ppublish
Résumé
Despite being the most abundantly secreted immunoglobulin isotype, the pattern of reactivity of immunoglobulin A (IgA) antibodies toward each individual's own gut commensal bacteria still remains elusive. By colonizing germ-free mice with defined commensal bacteria, we found that the binding specificity of bulk fecal and serum IgA toward resident gut bacteria resolves well at the species level and has modest strain-level specificity. IgA hybridomas generated from lamina propria B cells of gnotobiotic mice showed that most IgA clones recognized a single bacterial species, whereas a small portion displayed cross-reactivity. Orally administered hybridoma-produced IgAs still retained bacterial antigen binding capability, implying the potential for a new class of therapeutic antibodies. Species-specific IgAs had a range of strain specificities. Given the distinctive bacterial species and strain composition found in each individual's gut, our findings suggest the IgA antibody repertoire is shaped uniquely to bind "self" gut bacteria.
Identifiants
pubmed: 35857580
doi: 10.1126/sciimmunol.abg3208
pmc: PMC9421563
mid: NIHMS1828286
doi:
Substances chimiques
Immunoglobulin A
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
eabg3208Subventions
Organisme : NIDDK NIH HHS
ID : R01 DK112978
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK123749
Pays : United States
Organisme : NIDDK NIH HHS
ID : R01 DK124133
Pays : United States
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