Cross-Reactivity of Human Immunoglobulin G2 Recognizing Phosphorylcholine and Evidence for Protection against Major Bacterial Pathogens of the Human Respiratory Tract

Phosphorylcholine (ChoP) is an antigenic component on the cell surface of many commensal and pathogenic bacteria that reside in the upper airway. In the present study, human ChoP-specific antibody was affinitypurified from pooled serum gamma globulin. This naturally acquired antibody, which is prima...

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Bibliographic Details
Published in:The Journal of infectious diseases 2004-10, Vol.190 (7), p.1254-1263
Main Authors: Goldenberg, Hannah B., McCool, Tera L., Weiser, Jeffrey N.
Format: Article
Language:English
Subjects:
Antibodies
Antibodies, Bacterial - immunology
Antigens
Bacteria
Bacterial Vaccines - immunology
Bacteriology
Biological and medical sciences
Cross Reactions
Fundamental and applied biological sciences. Psychology
Haemophilus influenzae
Haemophilus influenzae - immunology
Humans
Immunoglobulin G - immunology
Infections
Infectious diseases
Medical sciences
Mice
Microbiology
Miscellaneous
Monoclonal antibodies
Pathogens
Phosphorylcholine - immunology
Streptococcus pneumoniae
Streptococcus pneumoniae - immunology
Teichoic acids
Vaccination
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Summary:Phosphorylcholine (ChoP) is an antigenic component on the cell surface of many commensal and pathogenic bacteria that reside in the upper airway. In the present study, human ChoP-specific antibody was affinitypurified from pooled serum gamma globulin. This naturally acquired antibody, which is primarily of the immunoglobulin (Ig) G2 subtype, recognized ChoP on the lipoteichoic acid of Streptococcus pneumoniae and on the lipopolysaccharide of Haemophilus influenzae, 2 of the leading etiologic agents of infection involving the human respiratory tract. In in vitro killing assays, anti-ChoP IgG2 was effective against some clinical isolates of nontypeable H. influenzae and against isolates of several common serotypes of S. pneumoniae. Moreover, passively administered human anti-ChoP antibody protected mice against lethal challenge with a transparent isolate of S. pneumoniae type 6A. The effectiveness of human antibody to this conserved bacterial structure suggests that, if it can be manipulated to broaden its activity, it could function as a single vaccine antigen that targets multiple pathogens.
ISSN:0022-1899
1537-6613
DOI:10.1086/424517