Mucoid strains of Pseudomonas aeruginosa are the major pulmonary pathogens for cystic fibrosis patients. Opsonizing antibodies to the mucoid exopolysaccharide (MEP) antigen may protect animals and some cystic fibrosis patients from infection. However, MEP does not readily elicit opsonic antibodies either during chronic infection or after vaccination. To evaluate alternative means to induce opsonic antibodies, a murine monoclonal anti-idiotypic antibody directed to an opsonic monoclonal antibody specific to MEP was produced. The anti-idiotypic antibody bound to F(ab')2 fragments of the opsonic antibody, blocked binding to MEP, bound to cross-reactive idiotopes on human opsonic antibodies to MEP, and elicited MEP-specific antibodies in syngeneic and allogeneic mice. These anti-idiotype-induced, MEP-specific antibodies fixed complement to mucoid P. aeruginosa cells and opsonized them for phagocytic killing by human leukocytes. These studies demonstrate the potential utility of anti-idiotypic monoclonal antibody for generating protective immunity against bacterial polysaccharides.

Download full-text PDF

Source
http://dx.doi.org/10.1093/infdis/164.3.507DOI Listing

Publication Analysis

Top Keywords

opsonic antibodies
16
monoclonal antibody
12
pseudomonas aeruginosa
8
mucoid exopolysaccharide
8
anti-idiotypic monoclonal
8
cystic fibrosis
8
fibrosis patients
8
anti-idiotypic antibody
8
mep-specific antibodies
8
antibodies
7

Similar Publications

Antibody-recruiting molecules (ARMs) have emerged as a promising strategy for enhancing immune responses against pathogens and cancer cells. In this study, we developed a novel class of antibacterial ARMs utilizing siderophores, small iron-chelating compounds, as targeting motifs. Siderophores naturally exhibit high specificity for bacterial pathogens due to their role in iron acquisition, making them ideal candidates for selective targeting.

View Article and Find Full Text PDF

Background: CD3 bispecific antibody (CD3 bsAb) therapy has become an established treatment modality for some cancer types and exploits endogenous T cells irrespective of their specificity. However, durable clinical responses are hampered by immune escape through loss of tumor target antigen expression. Induction of long-lasting tumor-specific immunity might therefore improve therapeutic efficacy, but has not been studied in detail yet for CD3 bsAbs.

View Article and Find Full Text PDF

Monoclonal antibodies (mAbs) improve survival of patients with mature B-cell malignancies. Fcγ-receptor dependent effector mechanisms kill tumor cells but can promote antigen loss through trogocytosis, contributing to treatment failures. Cell-bound mAbs trigger the complement cascade to deposit C3 activation fragments and lyse cells.

View Article and Find Full Text PDF
Article Synopsis
  • Dengue virus (DENV) is a significant global health issue, with severe cases potentially worsened by antibodies that can enhance infection rather than neutralize it.
  • Researchers are exploring the possibility of targeting DENV-infected cells for immune clearance to avoid antibody-dependent enhancement (ADE).
  • This study found that DENV structural proteins are present on infected cell surfaces and can be recognized by immune antibodies, which may facilitate the clearance of infected cells without enriching viral material in certain immune cells.
View Article and Find Full Text PDF

Acquisition of Fc-afucosylation of PfEMP1-specific IgG is age-dependent and associated with clinical protection against malaria.

Nat Commun

January 2025

Centre for translational Medicine and Parasitology, Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.

Protective immunity to malaria depends on acquisition of parasite-specific antibodies, with Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) being one of the most important target antigens. The effector functions of PfEMP1-specific IgG include inhibition of infected erythrocyte (IE) sequestration and opsonization of IEs for cell-mediated destruction. IgG glycosylation modulates antibody functionality, with increased affinity to FcγRIIIa for IgG lacking fucose in the Fc region (Fc-afucosylation).

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!