Antibodies to Escherichia coli 06 porins cross-react with urinary pathogens

Immunobiology
M KawaharaG J Domingue

Abstract

Antibodies to partially purified E. coli 06 35-40 KDa porin trimers recognized the reactive epitopes in the intact porin surface molecule present in various wild-type, heterologous, urinary pathogens. The presence of lipopolysaccharide in the membrane did not shield the antibody binding sites. The reactivity was shown to be specific for porins since LPS-absorbed porin antisera reacted with porins on immunoblots and showed no reactivity with LPS. Additionally, the cross-reactions were abolished by absorption of the porin antisera with E. coli 06 containing porin trimers. These data strengthen the rationale for exploring the enhancement of immunoprotection by monoclonal antibodies to specific immunoreactive antigens in the porin molecule.

References

Jun 1, 1989·APMIS : Acta Pathologica, Microbiologica, Et Immunologica Scandinavica·A Z HenriksenO G Brakstad
Dec 1, 1988·Kidney International·G J DomingueS C Li
Jan 1, 1985·Infection·L HagbergC Svanborg Edén
Feb 1, 1980·Journal of Medical Microbiology·H J BrooksW R Cattell

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Citations

May 12, 2000·European Journal of Biochemistry·M P MolloyA A Gooley

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