Purification and seroreactivity of pneumococcal surface adhesin A (PsaA).
AUTOR(ES)
Tharpe, J A
RESUMO
Pneumococcal surface adhesin A (PsaA) is a 37-kDa common protein antigen of Streptococcus pneumoniae. In the present study, the protein was purified so that its immunoreactivity could be determined. PsaA was released and purified from cells by lysis in the presence of n-laurylsarcosine; this was followed by ammonium sulfate precipitation and subsequent preparative isoelectric focusing. A capture antibody enzyme-linked immunosorbent assay was used to determine the immunoreactivity of purified PsaA. The assay had a 67% sensitivity for sera from patients with bacteremic pneumococcal pneumonia. A specificity of 97% was estimated on the basis of a lack of reactivity with sera from patients with pneumonia caused by other organisms. PsaA is a potential vaccine candidate and may be useful as an antigen in a diagnostic assay for pneumococcal disease.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=170284Documentos Relacionados
- Identification of the psaA Gene, Coding for Pneumococcal Surface Adhesin A, in Viridans Group Streptococci other than Streptococcus pneumoniae
- Limited diversity of Streptococcus pneumoniae psaA among pneumococcal vaccine serotypes.
- Conformational analysis of Pneumococcal Surface Antigen A (PsaA) upon zinc binding by fluorescence spectroscopy
- Cloning, expression and purification of proteins of surface, PsaA and fragments of PspA from Streptococcus pneumoniae
- Identification of Lipoprotein Homologues of Pneumococcal PsaA in the Equine Pathogens Streptococcus equi and Streptococcus zooepidemicus