Joseph J. Campo, United States of America
Antigen Discovery Inc. Antigen Discovery Inc.Author Of 1 Presentation
THE MUCOSAL AND SYSTEMIC ANTIBODY REPERTOIRE FOLLOWING EXPERIMENTAL PNEUMOCOCCAL CHALLENGE IN HEALTHY ADULTS (ID 993)
- Joseph J. Campo, United States of America
- Carla Solorzano, United Kingdom
- Esther L. German, United Kingdom
- Jesus Reine, United Kingdom
- Sherin Pojar, United Kingdom
- Elissavet Nikolaou, United Kingdom
- Elena Mitsi, United Kingdom
- Timothy Q. Le, United States of America
- Xiaowu Liang, United States of America
- Daniela M. Ferreira, United Kingdom
Abstract
Background
In the experimental human pneumococcal challenge (EHPC) model, healthy adults are intranasally inoculated with a pneumococcal challenge strain. A panproteome Streptococcus pneumoniae array, containing over 2,600 pneumococcal proteins, was used to screen systemic and mucosal antibodies from EHPC volunteers.
Methods
IgG and IgA responses were profiled in a cohort of 150 volunteers challenged with serotype 6B pneumococci, half of whom were susceptible to experimental colonization and the other half remained protected. Serum and nasal wash samples collected pre- and post-EHPC were probed on the S. pneumoniae panproteome microarray with simultaneous detection of IgA and IgG binding.
Results
Hundreds of pneumococcal proteins were reactive with serum and nasal wash IgG and IgA. IgA- and IgG-reactive proteins showed high levels of overlap. However, over 200 proteins were reactive only with IgG. Antibodies against numerous proteins significantly increased following challenge. Unsupervised clustering showed subject-specific stability of antibody profiles in serum, but independently grouped profiles in nasal wash samples collected before and after challenge. No specific profile differences were observed in pre-EHPC samples between susceptible and protected groups, but the response to EHPC showed unique antigen reactivity patterns.
Conclusions
A single encounter with pneumococci can elicit broad changes in mucosal and systemic antibody responses to pneumococcal proteins.
Presenter of 1 Presentation
THE MUCOSAL AND SYSTEMIC ANTIBODY REPERTOIRE FOLLOWING EXPERIMENTAL PNEUMOCOCCAL CHALLENGE IN HEALTHY ADULTS (ID 993)
- Joseph J. Campo, United States of America
- Carla Solorzano, United Kingdom
- Esther L. German, United Kingdom
- Jesus Reine, United Kingdom
- Sherin Pojar, United Kingdom
- Elissavet Nikolaou, United Kingdom
- Elena Mitsi, United Kingdom
- Timothy Q. Le, United States of America
- Xiaowu Liang, United States of America
- Daniela M. Ferreira, United Kingdom
Abstract
Background
In the experimental human pneumococcal challenge (EHPC) model, healthy adults are intranasally inoculated with a pneumococcal challenge strain. A panproteome Streptococcus pneumoniae array, containing over 2,600 pneumococcal proteins, was used to screen systemic and mucosal antibodies from EHPC volunteers.
Methods
IgG and IgA responses were profiled in a cohort of 150 volunteers challenged with serotype 6B pneumococci, half of whom were susceptible to experimental colonization and the other half remained protected. Serum and nasal wash samples collected pre- and post-EHPC were probed on the S. pneumoniae panproteome microarray with simultaneous detection of IgA and IgG binding.
Results
Hundreds of pneumococcal proteins were reactive with serum and nasal wash IgG and IgA. IgA- and IgG-reactive proteins showed high levels of overlap. However, over 200 proteins were reactive only with IgG. Antibodies against numerous proteins significantly increased following challenge. Unsupervised clustering showed subject-specific stability of antibody profiles in serum, but independently grouped profiles in nasal wash samples collected before and after challenge. No specific profile differences were observed in pre-EHPC samples between susceptible and protected groups, but the response to EHPC showed unique antigen reactivity patterns.
Conclusions
A single encounter with pneumococci can elicit broad changes in mucosal and systemic antibody responses to pneumococcal proteins.