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Mutations affecting antigenic determinants of an outer membrane protein of Escherichia coli.
Author(s) -
Desaymard C.,
Débarbouillé M.,
Jolit M.,
Schwartz M.
Publication year - 1986
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1986.tb04371.x
Subject(s) - biology , escherichia coli , bacterial outer membrane , escherichia coli proteins , antigen , genetics , membrane protein , enterobacteriaceae , escherichia , epitope , mutation , microbiology and biotechnology , gene , membrane
The Escherichia coli LamB protein is located in the outer membrane. It is both a component of the maltose and maltodextrin transport system, and the receptor for phages lambda and K10. It is a trimer composed of three identical polypeptide chains, each containing 421 residues. Six independent mutants have been isolated, in which the LamB protein is altered in its interaction with one or more monoclonal antibodies specific for regions of the protein that are exposed at the cell surface. Some of the mutations also altered the binding site for phage lambda. All of the mutations were clustered in the same region of the lamB gene, corresponding to residues 333‐394 in the polypeptide. This and previous results strongly suggest that a rather large segment of the LamB polypeptide, extending from residue 315 to 401, is exposed at the outer face of the outer membrane. This segment would bear the epitopes for the four available anti‐LamB monoclonal antibodies that react with the cell surface, and part of the binding site for phage lambda.