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Pneumococcal surface adhesin A of Streptococcus pneumoniae analyzed.
2004 JAN 7 - (NewsRx.com & NewsRx.net) -- Scientists report the results of an analysis of recombinant acylated pneumococcal surface adhesin A of Streptococcus pneumoniae by mass spectrometry in a recent issue of the Archives of Biochemistry and Biophysics.
"Streptococcus pneumoniae pneumococcal surface adhesin A (PsaA) is a species-common, immunogenic surface lipoprotein. In this study, the psaA gene was expressed as a nonfusion acylated protein in an Escherichia coli expression system. Yields of pure recombinant PsaA (rPsaA) were 8-10 mg/L of fermentation culture," investigators in the United States report.
"Analysis of rPsaA tryptic digests by HPLC-electrospray mass spectrometry (MS) confirmed 98% of the expected protein sequence," stated Barun K. De and colleagues at the Centers for Disease Control and Prevention. "GUMS data demonstrated very similar acylation of native and rPsaA by C12:0-C22:0 fatty acids, with C16 and C18 predominating. Negative ion electrospray MS/MS analysis of the rPsaA lipid anchor released by Pronase-E confirmed that the structure was based on an N-terminal palmitoylcysteine (Pam[subscript]3Cys)."
"Electrospray MS heterogeneity analysis of intact rPsaA indicated that all of the observed heterogeneity ...
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Source: HighBeam Research, Pneumococcal surface adhesin A of Streptococcus pneumoniae analyzed.