Identification of Borrelia burgdorferi Ribosomal Protein L25 by the Phage Surface Display Method and Evaluation of the Protein's Value for Serodiagnosis
M Mueller, S Bunk, I Diterich, M Weichel… - Journal of clinical …, 2006 - Am Soc Microbiol
M Mueller, S Bunk, I Diterich, M Weichel, C Rauter, D Hassler, C Hermann, R Crameri…
Journal of clinical microbiology, 2006•Am Soc MicrobiolThe phage surface display technique was used to identify Borrelia burgdorferi antigens. By
affinity selection with immunoglobulin G from pooled sera of six Lyme borreliosis (LB)
patients, the ribosomal protein L25 was identified. The diagnostic value of L25 was
investigated by an enzyme-linked immunosorbent assay, using sera from 80 LB patients and
75 controls, and the use of the protein resulted in a specificity of 99% and a 23% sensitivity,
which qualify L25 as a useful antigen when combined with others.
affinity selection with immunoglobulin G from pooled sera of six Lyme borreliosis (LB)
patients, the ribosomal protein L25 was identified. The diagnostic value of L25 was
investigated by an enzyme-linked immunosorbent assay, using sera from 80 LB patients and
75 controls, and the use of the protein resulted in a specificity of 99% and a 23% sensitivity,
which qualify L25 as a useful antigen when combined with others.
Abstract
The phage surface display technique was used to identify Borrelia burgdorferi antigens. By affinity selection with immunoglobulin G from pooled sera of six Lyme borreliosis (LB) patients, the ribosomal protein L25 was identified. The diagnostic value of L25 was investigated by an enzyme-linked immunosorbent assay, using sera from 80 LB patients and 75 controls, and the use of the protein resulted in a specificity of 99% and a 23% sensitivity, which qualify L25 as a useful antigen when combined with others.
American Society for Microbiology