Advanced

Human complement activation by smooth and rough Proteus mirabilis lipopolysaccharides

Kaca, Wieslaw; Arabski, Michal; Fudala, Rafal; Holmström, Eva M LU ; Sjöholm, Anders LU ; Weintraub, Andrej; Futoma-Koloch, Bozena; Bugla-Ploskonska, Gabriela and Doroszkiewicz, Wlodzimierz (2009) In Archivum Immunologiae et Therapiae Experimentalis 57(5). p.383-391
Abstract
Proteus mirabilis bacilli play an important role in human urinary tract infections, bacteremia, and rheumatoid arthritis. The authors previously studied human complement C3 conversion by smooth-form P. mirabilis O10, O23, O30, and O43 lipopolysaccharides (LPSs) and showed that smooth Proteus LPSs fragmented C3 in a dose- and time-dependent manner. In the present study, one smooth P. mirabilis S1959 and its two polysaccharide-truncated LPSs isolated from an R mutant strain were used to study the C3 conversion. The conversion of C3 to C3c by smooth and rough P. mirabilis LPSs was studied by capture ELISA and crossed immunoelectrophoresis. Proteins isolated from the outer membrane were analyzed by discontinuous sodium dodecyl sulfate gel... (More)
Proteus mirabilis bacilli play an important role in human urinary tract infections, bacteremia, and rheumatoid arthritis. The authors previously studied human complement C3 conversion by smooth-form P. mirabilis O10, O23, O30, and O43 lipopolysaccharides (LPSs) and showed that smooth Proteus LPSs fragmented C3 in a dose- and time-dependent manner. In the present study, one smooth P. mirabilis S1959 and its two polysaccharide-truncated LPSs isolated from an R mutant strain were used to study the C3 conversion. The conversion of C3 to C3c by smooth and rough P. mirabilis LPSs was studied by capture ELISA and crossed immunoelectrophoresis. Proteins isolated from the outer membrane were analyzed by discontinuous sodium dodecyl sulfate gel electrophoresis. The smooth P. mirabilis S1959 (O3) strain was resistant to the bactericidal activity of human serum, in contrast to the Ra and Re mutant strains. The presence of an exposed core oligosaccharide in R110 LPS was not sufficient to protect the strain from serum-dependent killing. In addition to LPS structure, the outer-membrane proteins may also play roles in protecting the smooth P. mirabilis S1959 (O3) strain from the bactericidal action of serum. It was shown that the Ra P. mirabilis R110 and the Re P. mirabilis R45 mutants possess very different OMP compositions from that of the P. mirabilis S 1959 strain. Regardless of the complement resistance of the P. mirabilis strains, the S1959, R110, and R45 LPSs fragmented C3 and induced C3c neo-antigen exposure. The use of complement-deficient human serum allows the conclusion that the Re-type P. mirabilis R45 LPS fragmented C3 by the antibody-independent classical pathway. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
lipopolysaccharide, Proteus mirabilis, complement, outer-membrane, protein
in
Archivum Immunologiae et Therapiae Experimentalis
volume
57
issue
5
pages
383 - 391
publisher
Birkhaüser
external identifiers
  • wos:000269319300008
  • scopus:69549114276
ISSN
0004-069X
DOI
10.1007/s00005-009-0043-8
language
English
LU publication?
yes
id
deb0e631-5be1-4f3e-b85a-5cbc35d688d3 (old id 1476805)
date added to LUP
2009-09-25 09:00:15
date last changed
2017-10-01 04:09:09
@article{deb0e631-5be1-4f3e-b85a-5cbc35d688d3,
  abstract     = {Proteus mirabilis bacilli play an important role in human urinary tract infections, bacteremia, and rheumatoid arthritis. The authors previously studied human complement C3 conversion by smooth-form P. mirabilis O10, O23, O30, and O43 lipopolysaccharides (LPSs) and showed that smooth Proteus LPSs fragmented C3 in a dose- and time-dependent manner. In the present study, one smooth P. mirabilis S1959 and its two polysaccharide-truncated LPSs isolated from an R mutant strain were used to study the C3 conversion. The conversion of C3 to C3c by smooth and rough P. mirabilis LPSs was studied by capture ELISA and crossed immunoelectrophoresis. Proteins isolated from the outer membrane were analyzed by discontinuous sodium dodecyl sulfate gel electrophoresis. The smooth P. mirabilis S1959 (O3) strain was resistant to the bactericidal activity of human serum, in contrast to the Ra and Re mutant strains. The presence of an exposed core oligosaccharide in R110 LPS was not sufficient to protect the strain from serum-dependent killing. In addition to LPS structure, the outer-membrane proteins may also play roles in protecting the smooth P. mirabilis S1959 (O3) strain from the bactericidal action of serum. It was shown that the Ra P. mirabilis R110 and the Re P. mirabilis R45 mutants possess very different OMP compositions from that of the P. mirabilis S 1959 strain. Regardless of the complement resistance of the P. mirabilis strains, the S1959, R110, and R45 LPSs fragmented C3 and induced C3c neo-antigen exposure. The use of complement-deficient human serum allows the conclusion that the Re-type P. mirabilis R45 LPS fragmented C3 by the antibody-independent classical pathway.},
  author       = {Kaca, Wieslaw and Arabski, Michal and Fudala, Rafal and Holmström, Eva M and Sjöholm, Anders and Weintraub, Andrej and Futoma-Koloch, Bozena and Bugla-Ploskonska, Gabriela and Doroszkiewicz, Wlodzimierz},
  issn         = {0004-069X},
  keyword      = {lipopolysaccharide,Proteus mirabilis,complement,outer-membrane,protein},
  language     = {eng},
  number       = {5},
  pages        = {383--391},
  publisher    = {Birkhaüser},
  series       = {Archivum Immunologiae et Therapiae Experimentalis},
  title        = {Human complement activation by smooth and rough Proteus mirabilis lipopolysaccharides},
  url          = {http://dx.doi.org/10.1007/s00005-009-0043-8},
  volume       = {57},
  year         = {2009},
}