Crucial domains are conserved in Enterobacteriaceae porins

Abstract With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-pep...

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Bibliographic Details
Published in:FEMS microbiology letters 1996-02, Vol.136 (1), p.91-97
Main Authors: Simonet, Valérie, Malléa, Monique, Fourel, Didier, Bolla, Jean-Michel, Pages, Jean-Marie
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibiotic resistance
Antibodies
Antigens
Antigens, Bacterial - chemistry
Antigens, Bacterial - genetics
Anti‐peptide antibodies
Bacteria
Bacterial porins
Bacteriology
Biological and medical sciences
Conserved Sequence
Cross Reactions
Crystal structure
Domains
E coli
Enterobacteriaceae
Enterobacteriaceae - genetics
Enterobacteriaceae - immunology
Epitopes
Escherichia coli
Escherichia coli - genetics
Escherichia coli - immunology
Functional morphology
Fundamental and applied biological sciences. Psychology
Gram-negative bacteria
Gram-Negative Bacteria - genetics
Gram-Negative Bacteria - immunology
Immunochemistry
Microbiology
Molecular Sequence Data
Molecular Structure
Mutagenesis, Site-Directed
Peptides
Permeability, membrane transport, intracellular transport
Plasmids
Pore formation
Porins
Porins - chemistry
Porins - genetics
Porins - immunology
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Summary:Abstract With the recent resolution of the crystal structures of several bacterial porins, it is worthwhile to define the generality of their organization throughout the Enterobacteriaceae. The distribution of specific epitopes was analysed among various Gram-negative bacterial porins using anti-peptide antibodies specific to exposed, transmembrane spanning, or pore-forming regions of Escherichia coli porins. Anti-peptide antibodies which recognized the exposed epitopes indicated a great variability among the bacterial porins analysed. Interestingly, an antigenic site located in the internal loop L3 constricting the pore diameter was present in the majority of the bacterial porins tested. Two epitopes located in domains involved in subunit interaction were also highly conserved. The presence of these common peptides suggested a conservation of specific regions involved in the functional organization of the enterobacterial porins.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1996.tb08030.x