Interaction of Klebsiella capsule type 7 with human polymorphonuclear leucocytes

Microb Pathog. 1992 Nov;13(5):371-9. doi: 10.1016/0882-4010(92)90080-8.

Abstract

Klebsiella serotype K7 is found among the capsule types that are most prevalent in respiratory tract isolates. To evaluate the significance of the K7 antigen in bacteria-leucocyte interactions, K7-encapsulated Klebsiella pneumoniae strains and their non-capsulate mutants were investigated. The K7 isolates were compared to K2-capsulate strains and their respective K- derivatives. K7-capsulate bacteria were less hydrophilic, and more readily phagocytosed and killed by human polymorphonuclear leucocytes (PMNL) than K2 strains. Loss of the K7 antigen resulted in increased surface hydrophobicity but did not affect phagocytosis and killing, whereas loss of the K2 capsule caused greater susceptibility to the phagocytic and killing action of PMNL. Both the K7 and K2 antigen stimulated the extracellular release of lysozyme from neutrophils but not of myeloperoxidase, indicating degranulation of only secondary granules. All K- mutants induced the release of both lysozyme and myeloperoxidase. Our results suggest that, in contrast to the K2 antigen, the K7 capsular polysaccharide does not confer antiphagocytic properties on bacteria. However, the K7 antigen is able to impede the extracellular release of primary granule enzymes.

MeSH terms

  • Antigens, Bacterial / immunology
  • Antigens, Bacterial / metabolism
  • Bacterial Capsules
  • Humans
  • Klebsiella / genetics
  • Klebsiella / metabolism*
  • Klebsiella / pathogenicity
  • Luminescent Measurements
  • Lysosomes / enzymology
  • Muramidase / metabolism
  • Mutation
  • Neutrophils / immunology
  • Neutrophils / metabolism*
  • Peroxidase / metabolism
  • Phagocytosis
  • Polysaccharides, Bacterial / immunology
  • Polysaccharides, Bacterial / metabolism*

Substances

  • Antigens, Bacterial
  • Polysaccharides, Bacterial
  • capsular polysaccharide K2
  • capsular polysaccharide K7
  • Peroxidase
  • Muramidase