Characterization of outer membrane proteins of virulent phase I Shigella sonnei strains and their avirulent phase I derivatives.

Grazyna Adamus, M. Mulczyk, D. Witkowska

Research output: Contribution to journalArticle

Abstract

Comparison of polyacrylamide gel electrophoretic protein profiles of four isogenic sets of virulent phase I Sh. sonnei strains and their avirulent phase I cells revealed no differences in outer membrane protein composition between virulent and avirulent derivatives. However, significant qualitative and quantitative differences were found in composition of major outer membrane proteins between strains of different origin. All four strains tested contained one major protein of 33K. This protein was susceptible to proteolytic enzymes and was found to be heat modifiable. Other major proteins of 35K and 37K present in three strains and 36K present in one strain were identified as peptidoglycan associated proteins.

Original languageEnglish (US)
Pages (from-to)513-516
Number of pages4
JournalArchivum Immunologiae et Therapiae Experimentalis
Volume34
Issue number5-6
StatePublished - 1986
Externally publishedYes

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Shigella sonnei
Membrane Proteins
Proteins
Peptidoglycan
Peptide Hydrolases
Hot Temperature

ASJC Scopus subject areas

  • Immunology

Cite this

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abstract = "Comparison of polyacrylamide gel electrophoretic protein profiles of four isogenic sets of virulent phase I Sh. sonnei strains and their avirulent phase I cells revealed no differences in outer membrane protein composition between virulent and avirulent derivatives. However, significant qualitative and quantitative differences were found in composition of major outer membrane proteins between strains of different origin. All four strains tested contained one major protein of 33K. This protein was susceptible to proteolytic enzymes and was found to be heat modifiable. Other major proteins of 35K and 37K present in three strains and 36K present in one strain were identified as peptidoglycan associated proteins.",
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AU - Witkowska, D.

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