Factor H and neisserial pathogenesis

Vaccine. 2008 Dec 30;26 Suppl 8(Suppl 8):I40-5. doi: 10.1016/j.vaccine.2008.11.060.


Both Neisseria gonorrhoeae and N. meningitidis bind to factor H which enhances their ability to evade complement-dependent killing. While porin is the ligand for human fH on gonococci, meningococci use a lipoprotein called factor H binding protein (fHbp) to bind to factor H and enhance their ability to evade complement-dependent killing. This protein is currently being intensively investigated as a meningococcal vaccine candidate antigen. Consistent with the observation that meningococci cause natural infection only in humans, the organism resists human complement, and are more readily killed by complement from lower animals. This human species-specific complement evasion has important implications for evaluation of vaccine-elicited antibodies using non-human complement sources and development of animal models of disease.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Antigens, Bacterial / immunology
  • Bacterial Proteins / immunology
  • Blood Bactericidal Activity
  • Complement Factor H / physiology*
  • Complement System Proteins / deficiency
  • Gonorrhea / etiology*
  • Gonorrhea / immunology
  • Humans
  • Ligands
  • Lipopolysaccharides / metabolism
  • Meningococcal Infections / etiology*
  • Meningococcal Infections / immunology
  • Meningococcal Vaccines / immunology
  • N-Acetylneuraminic Acid / metabolism
  • Neisseria gonorrhoeae / immunology*
  • Neisseria gonorrhoeae / pathogenicity
  • Neisseria meningitidis / immunology*
  • Neisseria meningitidis / pathogenicity
  • Species Specificity


  • Antigens, Bacterial
  • Bacterial Proteins
  • Ligands
  • Lipopolysaccharides
  • Meningococcal Vaccines
  • factor H-binding protein, Neisseria meningitidis
  • lipid-linked oligosaccharides
  • Complement Factor H
  • Complement System Proteins
  • N-Acetylneuraminic Acid