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Major outer membrane proteins of E. coli K12 serve as receptors for the phages T2 (protein Ia) and 434 (protein Ib)

โœ Scribed by Hantke, K.

Publisher
Springer
Year
1978
Tongue
English
Weight
460 KB
Volume
164
Category
Article
ISSN
0026-8925

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โœฆ Synopsis

Mutants of E. coli resistant to bacteriophage T2 have lowered amounts of protein Ia in their outer membrane. Bacteriophage T2 was inactivated by a mixture of protein Ia-lipopolysaccharide. Protein Ia or lipopolysaccharide alone had no neutralizing activity. However, only protein Ia was required to inactivate a T2 host range mutant. In the presence of polymyxin B T2 receptor activity of protein Ia--lipopolysaccharide mixtures could not be restored. E. coli strains missing protein Ib were resistant against the lambdoid phage 434. Purified protein Ib inactivated 434 and lambdavirh434. Addition of lipopolysaccharide did not enhance the neutralizing activity of protein Ib, indicating that lipopolysaccharide may not be necessary for the inactivation of the phage.

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Sequence of the regulatory region of omp
Sequence of the regulatory region of ompT, the gene specifying major outer membrane protein a (3b) of Escherichia coli K-12: Implications for regulation and processing
โœ Gordon, Gerald ;Gayda, Randall C. ;Markovitz, Alvin ๐Ÿ“‚ Article ๐Ÿ“… 1984 ๐Ÿ› Springer ๐ŸŒ English โš– 823 KB

The DNA of the promoter region of omp T, including the putative start for the pro-Omp T protein (pro-protein a), has been sequenced. Previous studies showed that trypsin inhibitors prevent the processing of pro-Omp T to Omp T protein which led to the prediction that the processing site would be a ly