Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model.

@article{VuopioVarkila1988ProtectiveCO,
  title={Protective capacity of antibodies to outer-membrane components of Escherichia coli in a systemic mouse peritonitis model.},
  author={Jaana Vuopio‐Varkila and M. Karvonen and Harri Saxén},
  journal={Journal of medical microbiology},
  year={1988},
  volume={25 2},
  pages={
          77-84
        }
}
Antibody-mediated protection was studied in an experimental murine model of peritonitis-septicaemia with Escherichia coli O18:K1. Protection from lethal intraperitoneal challenge was achieved by passive immunisation with horse anti-K1 capsular antiserum (H46) or rabbit antiserum to the homologous O18 antigen. The maximum increase in LD50 achieved with anti-K1 and anti-O18 antibodies was 10- and 5-fold, respectively. The protective capacity of the anti-O serum was found to be in the IgG fraction… 
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The data document the interdependent antibacterial and complement-fixing properties of LPS-reactive MAbs and the degree to which both activities are determined by antibody class and isotype.
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TLDR
A high degree of non-specific resistance to a lethal systemic Escherichia coli infection was induced in mice by pretreatment with a small dose of the homologous lipopolysaccharide (LPS) or with heterologous rough-type LPS from E. coli K-12, corresponding to the 100-fold reduced toxicity of MPL for mice and rabbits in lethality and pyrogenicity assays.
Review: Evidence against the hypothesis that antibodies to the inner core of lipopolysaccharides in antisera raised by immunization with enterobacterial deep-rough mutants confer broad-spectrum protection during Gram-negative bacterial sepsis
TLDR
This review summarizes experiments by the laboratory and others that do not confirm that binding and neutralization of lipopolysaccharides by antibodies to common core epitopes underlies broad-spectrum protection by rough-mutant antisera against wild-type smooth strains.
A strong antibody response to the periplasmic C-terminal domain of the OmpA protein of Escherichia coli is produced by immunization with purified OmpA or with whole E. coli or Salmonella typhimurium bacteria
TLDR
Because the ompA gene of enterobacteria is highly conserved, the Bac-OmpA might be useful as a group-specific EIA antigen to diagnose diseases caused by members of the family Enterobacteriaceae.
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TLDR
Results indicate that IML assays can detect smooth-type enterobacterial endotoxins in plasma and suggest that such assays have potential for use in the rapid diagnosis of sepsis and endotoxemia caused by different enterob bacterial species.
The C-Terminal Domain of Salmonella enterica Serovar Typhimurium OmpA Is an Immunodominant Antigen in Mice but Appears To Be Only Partially Exposed on the Bacterial Cell Surface
TLDR
The strong immunogenicity of this epitope was surprising because the C-terminal domain of OmpA, usually thought to be located in the periplasm, is not expected to be exposed on the bacterial cell surface, and is consistent with the proposal that OMPA can fold into one of the two alternate conformations.
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The utility of recombinant DNA technology for creating a panel of antibodies that may aid in selecting potential immunotherapeutic candidates is demonstrated by investigating the influence of valence and heavy chain on antibody activity.
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TLDR
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TLDR
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