title: Antibodies against four proteins from a Streptococcus pyogenes serotype M1 strain and levels of circulating mannan-binding lectin in acute poststreptococcal glomerulonephritis.
abstract: BACKGROUND
  Responses against antigens from the potentially nephritogenic Streptococcus pyogenes serotype M1 in patients with acute poststreptococcal glomerulonephritis (AGN) were studied to seek indications of expression of these antigens during the preceding infection. Also, the question was asked whether the complement protein mannan-binding lectin (MBL) is required for development of the hypocomplementemia associated with AGN. Hypothetically, the lectin pathway might trigger the alternative pathway, which is consistently activated in AGN.
  
  
  METHODS
  Antibodies against three proteins associated with M1, M1 protein, streptococcal inhibitor of complement (SIC) and protein H, an IgG-binding protein, were determined by ELISA in 56 children and 17 adults with AGN. Antibodies against streptococcal cysteine proteinase, which is produced by all serotypes of S. pyogenes, were also examined. MBL concentrations were measured in the same 71 patients by a sandwich ELISA.
  
  
  RESULTS
  Increased concentrations of antibodies were found against all four streptococcal proteins, albeit not uniformly distributed between different subgroups of patients. The prevalence of low MBL concentrations (<100 microg/l) including 2 patients with undetectable MBL (<10 microg/l) was similar in AGN (11%) and in controls (16%).
  
  
  CONCLUSIONS
  Our results give evidence of exposure to SIC and protein H in conjunction with AGN. This implies that SIC and protein H and/or cross-reacting proteins may have a role in the pathogenesis of AGN or that streptococci expressing SIC or protein H are nephritogenic for other reasons. The finding of MBL-deficient individuals among the patients demonstrates that MBL is not necessary for the recruitment of complement in AGN.
authors.affiliation: Section of Microbiology, Immunology and Glycobiology, Institute of Laboratory Medicine, Lund University, Lund, Sweden. lillemur.skattum@skane.se
authors.forename: L
authors.initials: L
authors.lastname: Skattum
authors.forename: P
authors.initials: P
authors.lastname: Akesson
authors.forename: L
authors.initials: L
authors.lastname: Truedsson
authors.forename: A G
authors.initials: AG
authors.lastname: Sjöholm
mesh_terms: D000293:Adolescent; D000328:Adult; D000907:Antibodies, Bacterial / Q000097:blood*; D000989:Antistreptolysin / Q000097:blood; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology*; D002352:Carrier Proteins / Q000276:immunology; D002648:Child; D003169:Complement Inactivator Proteins / Q000276:immunology; D003851:Deoxyribonucleases / Q000276:immunology; D005260:Female; D005921:Glomerulonephritis / Q000097:blood / Q000276:immunology* / Q000382:microbiology; D006801:Humans; D008297:Male; D037601:Mannose-Binding Lectin / Q000097:blood* / Q000172:deficiency; D008565:Membrane Proteins / Q000276:immunology; D013290:Streptococcal Infections / Q000097:blood / Q000276:immunology* / Q000382:microbiology; D013297:Streptococcus pyogenes / Q000276:immunology*
chemical_list: D000907:Antibodies, Bacterial; D001426:Bacterial Proteins; D002352:Carrier Proteins; D003169:Complement Inactivator Proteins; D037601:Mannose-Binding Lectin; D008565:Membrane Proteins; C097739:SIC protein, Streptococcus; C064006:protein H, Streptococcus; D000989:Antistreptolysin; D003851:Deoxyribonucleases; C020069:deoxyribonuclease B