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Major outer membrane protein in Salmonella typhimurium induced by maltose.

ABSTRACT

A maltose-induced major outer membrane protein (the 44K protein) is demonstrated in Salmonella typhimurium. This protein resembles the lambda receptor of Escherichia coli in its location, induction properties, apparent molecular weight, and association with the peptidoglycan layer of the cell wall. The 44K protein is missing in certain Salmonella Mal- mutants, which are also missing a protein analogous to the maltose-binding protein of E. coli. Thus, these mutants may be defective in the control of maltose genese in Salmonella. The proteins appear to be closely related, as indicated by cross-reaction of the Salmonella protein with the antiserum raised against the lambda receptor; however, they are not identical, since the peptide patterns obtained after limited proteolysis are completely different. Bacteriophage lambda does not use the 44K protein as a receptor.

This article has been cited by other articles:

• Orlik, F., Andersen, C., Benz, R. (2002). Site-Directed Mutagenesis of Tyrosine 118 within the Central Constriction Site of the LamB (Maltoporin) Channel of Escherichia coli. II. Effect on Maltose and Maltooligosaccharide Binding Kinetics. Biophys. J 83: 309-321 [Abstract] [Full Text]