Epitope mapping of pneumococcal surface protein A of strain Rx1 using monoclonal antibodies and molecular structure modelling

Jan Kolberg; Audun Aase; Gunnhild Rødal; James E Littlejohn; Mark J. Jedrzejas

doi:10.1016/S0928-8244(03)00255-4

Epitope mapping of pneumococcal surface protein A of strain Rx1 using monoclonal antibodies and molecular structure modelling

Jan Kolberg, Audun Aase, Gunnhild Rødal, James E Littlejohn, Mark J. Jedrzejas

Research output: Contribution to journal › Article

12 Scopus citations

Abstract

Pneumococcal surface protein A (PspA) is an antigenic variable vaccine candidate of Streptococcus pneumoniae. Epitope similarities between PspA from the American vaccine candidate strain Rx1 and Norwegian clinical isolates were studied using PspA specific monoclonal antibodies (mAbs) made against clinical Norwegian strains. Using recombinant PspA/Rx1 fragments and immunoblotting the epitopes for mAbs were mapped to two regions of amino acids, 1-67 and 67-236. The discovered epitopes were visualized by modelling of the PspA:Fab part of mAb in three dimensions. Flow cytometric analysis showed that the epitopes for majority of mAbs were accessible for antibody binding on live pneumococci. Also, the epitopes for majority of the mAbs are widely expressed among clinical Norwegian isolates.

Original language	English (US)
Pages (from-to)	265-273
Number of pages	9
Journal	FEMS Immunology and Medical Microbiology
Volume	39
Issue number	3
DOIs	https://doi.org/10.1016/S0928-8244(03)00255-4
State	Published - Dec 5 2003
Externally published	Yes

Keywords

Monoclonal antibody
Pneumococcal surface protein A
Pneumococcal vaccine
Streptococcus pneumoniae

ASJC Scopus subject areas

Immunology and Allergy
Microbiology
Immunology
Microbiology (medical)
Infectious Diseases

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Kolberg, J., Aase, A., Rødal, G., Littlejohn, J. E., & Jedrzejas, M. J. (2003). Epitope mapping of pneumococcal surface protein A of strain Rx1 using monoclonal antibodies and molecular structure modelling. FEMS Immunology and Medical Microbiology, 39(3), 265-273. https://doi.org/10.1016/S0928-8244(03)00255-4

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