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    <title>Kerr, A.</title>
    <link>http://repub.eur.nl/res/aut/12579/</link>
    <description>List of Publications</description>
    <language>en</language>
    <image>
      <url>http://repub.eur.nl/static-eur/img/logo.png</url>
      <title>RePub, Erasmus University Rotterdam</title>
      <link>http://repub.eur.nl</link>
    </image>
    <item>
      <title>The putative proteinase maturation protein A of Streptococcus pneumoniae is a conserved surface protein with potential to elicit protective immune responses (Article)</title>
      <link>http://repub.eur.nl/res/pub/9386/</link>
      <pubDate>2000-01-01T00:00:00Z</pubDate>
      <description>Surface-exposed proteins often play an important role in the interaction
          between pathogenic bacteria and their host. We isolated a pool of
          hydrophobic, surface-associated proteins of Streptococcus pneumoniae. The
          opsonophagocytic activity of hyperimmune serum raised against this protein
          fraction was high and species specific. Moreover, the opsonophagocytic
          activity was independent of the capsular type and chromosomal genotype of
          the pneumococcus. Since the opsonophagocytic activity is presumed to
          correlate with in vivo protection, these data indicate that the protein
          fraction has the potential to elicit species-specific immune protection
          with cross-protection against various pneumococcal strains. Individual
          proteins in the extract were purified by two-dimensional gel
          electrophoresis. Antibodies raised against three distinct proteins
          contributed to the opsonophagocytic activity of the serum. The proteins
          were identified by mass spectrometry and N-terminal amino acid sequencing.
          Two proteins were the previously characterized pneumococcal surface
          protein A and oligopeptide-binding lipoprotein AmiA. The third protein was
          the recently identified putative proteinase maturation protein A (PpmA),
          which showed homology to members of the family of peptidyl-prolyl
          cis/trans isomerases. Immunoelectron microscopy demonstrated that PpmA was
          associated with the pneumococcal surface. In addition, PpmA was shown to
          elicit species-specific opsonophagocytic antibodies that were
          cross-reactive with various pneumococcal strains. This antibody
          cross-reactivity was in line with the limited sequence variation of ppmA.
          The importance of PpmA in pneumococcal pathogenesis was demonstrated in a
          mouse pneumonia model. Pneumococcal ppmA-deficient mutants showed reduced
          virulence. The properties of PpmA reported here indicate its potential for
          inclusion in multicomponent protein vaccines.</description>
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