Molecular analysis of the pathogenicity of Streptococcus pneumoniae: the role of pneumococcal proteins

Annu Rev Microbiol. 1993;47:89-115. doi: 10.1146/annurev.mi.47.100193.000513.


For many years the virulence of Streptococcus pneumoniae has largely been attributed to its antiphagocytic polysaccharide capsule. Recent evidence, however, indicates that certain pneumococcal proteins play an important part in the pathogenesis of disease, either as mediators of inflammation or by directly attacking host tissues. Pneumococci carrying defined mutations in the genes encoding any one of at least three pneumococcal proteins (the toxin pneumolysin, the major pneumococcal autolysin, and pneumococcal surface protein A) have significantly reduced virulence. Pneumococcal hydrolytic enzymes, such as neuraminidase, hyaluronidase, and IgA1 protease may also contribute to colonization and/or invasion of the host. Several of these proteins (or their detoxified derivatives) are protective immunogens in animal models and therefore warrant consideration for inclusion in human antipneumococcal vaccine formulations.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / metabolism*
  • Bacterial Vaccines
  • Humans
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism
  • Neuraminidase / metabolism
  • Streptococcus pneumoniae / pathogenicity*
  • Streptolysins / metabolism


  • Bacterial Proteins
  • Bacterial Vaccines
  • Membrane Proteins
  • Streptolysins
  • plY protein, Streptococcus pneumoniae
  • Neuraminidase
  • N-Acetylmuramoyl-L-alanine Amidase