Features and protective efficacy of human mAbs targeting Mycobacterium tuberculosis arabinomannan.
Antigen
Immunoglobulins
Immunology
Infectious disease
Tuberculosis
Journal
JCI insight
ISSN: 2379-3708
Titre abrégé: JCI Insight
Pays: United States
ID NLM: 101676073
Informations de publication
Date de publication:
23 Oct 2023
23 Oct 2023
Historique:
received:
15
12
2022
accepted:
06
09
2023
medline:
3
11
2023
pubmed:
21
9
2023
entrez:
21
9
2023
Statut:
epublish
Résumé
A better understanding of the epitopes most relevant for antibody-mediated protection against tuberculosis (TB) remains a major knowledge gap. We have shown that human polyclonal IgG against the Mycobacterium tuberculosis (M. tuberculosis) surface glycan arabinomannan (AM) and related lipoarabinomannan (LAM) is protective against TB. To investigate the impact of AM epitope recognition and Fcγ receptor (FcγR) binding on antibody functions against M. tuberculosis, we isolated a high-affinity human monoclonal antibody (mAb; P1AM25) against AM and showed its binding to oligosaccharide (OS) motifs we previously found to be associated with in vitro functions of human polyclonal anti-AM IgG. Human IgG1 P1AM25, but not 2 other high-affinity human IgG1 anti-AM mAbs reactive with different AM OS motifs, enhanced M. tuberculosis phagocytosis by macrophages and reduced intracellular growth in an FcγR-dependent manner. P1AM25 in murine IgG2a, but neither murine IgG1 nor a non-FcγR-binding IgG, given intraperitoneally prior to and after aerosolized M. tuberculosis infection, was protective in C57BL/6 mice. Moreover, we demonstrated the protective efficacy of human IgG1 P1AM25 in passive transfer with M. tuberculosis-infected FcγR-humanized mice. These data enhance our knowledge of the important interplay between both antibody epitope specificity and Fc effector functions in the defense against M. tuberculosis and could inform development of vaccines against TB.
Identifiants
pubmed: 37733444
pii: 167960
doi: 10.1172/jci.insight.167960
pmc: PMC10619501
doi:
pii:
Substances chimiques
arabinomannan
53026-40-7
Receptors, IgG
0
Antibodies, Monoclonal
0
Immunoglobulin G
0
Epitopes
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
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