Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants

Bassford, P J; Diedrich, Dana L.; Schnaitman, C L; Reeves, Peter R.

doi:10.1128/jb.131.2.608-622.1977

Cited by 161 publications

(75 citation statements)

References 24 publications

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“…The composition of outer membrane proteins is affected with nutrient constituents in the growth medium in many bacteria (1,3,6,12). The previous work (9) showed that the SDS-PAGE profiles of outer membranes from V. vulnificus including various isolates from clinical and environmental sources vary according to the strain.…”

Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Three Porin‐Like Proteins from Vibrio vulnificus: Effect of Different Growth Media on Their Production

Koga

Takumi

1994

Microbiology and Immunology

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The effect of the culture media on the composition of the outer membrane protein of Vibrio vulnificus strain 393 from human blood was examined. Only one major outer membrane protein, with an apparent molecular weight of 37,000 (37K protein) and 34,000 (34K protein), was formed in the cells grown in 3% NaCl-BHI broth and chemically defined medium, respectively. The production of one major outer membrane protein was also observed in other isolates from humans and asari clam when they were grown in 3% NaCl-BHI broth. On the other hand, three major outer membrane proteins, with apparent molecular weights of 48,000 (48K protein), 37,000 (37K protein), and 34,000 (34K protein), were produced in the cells grown in 3% NaCl-nutrient broth. Three proteins, 48K, 37K, and 34K from strain 393, were purified and the amino acid compositions were determined. Although there was a little difference in the composition of amino acid among three proteins, the amino acid compositions of the three porin-like proteins showed characteristic properties of the porins of Escherichia coli and Salmonella typhimurium. Immunoblot analysis of the outer membrane proteins from four vibrios, E. coli, and S. typhimurium using monospecific antisera against these three porin-like proteins showed that only the antiserum against 37K protein cross-reacted with the outer membrane proteins from all the strains tested.Key words: Porin-like protein, Vibrio vulnificus Vibrio vulnificus, a halophilic marine bacterium, causes a number of extraintestinal infections. Septicemia caused by V. vulnificus is associated with underlying diseases including hemochromatosis, thalassemia, chronic cirrhosis and hepatoma (2). In view of the high correlation between V. vulnificus infections and diseases involving increased iron status, the effect of iron and iron-chelating agents upon the pathogenicity has been examined (18). In regard to the outer membrane, there are several papers describing the iron-regulated outer membrane proteins which are produced under the ironlimited conditions. However, the number of manuscript describing a porin which plays an essential role in the uptake of nutrition is limited. In a previous paper (9), we reported that the composition of outer membrane protein was affected by the composition of the media used for cultivation. In the present study, we cultured V. vulnificus strain 393 grown in 3% NaCl-brain heart infusion (BHI) broth, which are often used to cultivate the bacteria, and compared the composition of the outer membrane proteins with those of cells cultured in 3% NaCl-nutrient broth and in chemically defined medium. It became clear that the strain produces a new major outer membrane protein, the 37K protein, when it is grown in 3% NaCl-BHI broth. We also examined the outer membrane proteins from other V. vulnificus strains isolated from the blood of patients with septicemia, from seawater and from an asari clam grown in 3% NaCl-BHI broth.As strain 393 produces three porin-like proteins when they are cultured in 3% NaCl-nutri...

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Section: Discussionmentioning

confidence: 99%

Isolation and Characterization of Three Porin‐Like Proteins from Vibrio vulnificus: Effect of Different Growth Media on Their Production

Koga

Takumi

1994

Microbiology and Immunology

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“…We designate these as proteins la and lb (see reference 2 for other nomenclature systems). In addition, strains lysogenic for the lambdoid phage PA-2 produce large amounts of a different protein which we term protein 2 (22), and we have recently shown that this protein, which replaces proteins la and lb in lysogens, is also a porin.…”

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Identification of three genes controlling production of new outer membrane pore proteins in Escherichia coli K-12

Pugsley¹,

Schnaitman²

1978

J Bacteriol

123

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Escherichia coli K-12 strains carrying mutations in the ompB gene or double mutations in the tolF and par genes lack the major outer membrane proteins la and lb. These strains are deficient in the transport of small hydrophylic compounds and are multiply colicin resistant. When revertants of these strains were sought, a number of extragenic pseudorevertants were obtained which produced new outer membrane proteins. These new proteins could be divided into three classes by differences in electrophoretic mobility on polyacrylamide gels, by differing specificities for transport of small molecules, and by the identification of three different genetic loci for genes controlling their production. These genetic loci are designated as nmpA (at approximately 82.5 min on the E. coli K-12 genetic map), nmpB (8.6 min), and nmpC (12 min). The new proteins produced in strains carrying nmpA, nmpB, or nmpC mutations did not cross-react with antiserum against a mixture of proteins la and lb, or with antiserum against phage-directed protein 2. Production of the new membrane proteins restored sensitivity to some of the colicins. 1118 on July 31, 2020 by guest

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“…In most E. coli K-12 strains the major outer membrane protein of interest consists of two very similar polypeptides, Ia and lb (19; they are identical with la/lb [1], b/c [10], 0-9/0-8 [13], A1/A2 [17], 4 [20], and one of the two with the matrix protein [18]). In E. coli B/r only one such protein is present, and, as judged from its electrophoretic mobility and phage resistance pattern (see Table 1), it is polypeptide Ia.…”

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Two-component nature of bacteriophage T4 receptor activity in Escherichia coli K-12

Henning¹,

Jann²

1979

J Bacteriol

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Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants

Cited by 161 publications

References 24 publications

Isolation and Characterization of Three Porin‐Like Proteins from Vibrio vulnificus: Effect of Different Growth Media on Their Production

Isolation and Characterization of Three Porin‐Like Proteins from Vibrio vulnificus: Effect of Different Growth Media on Their Production

Identification of three genes controlling production of new outer membrane pore proteins in Escherichia coli K-12

Two-component nature of bacteriophage T4 receptor activity in Escherichia coli K-12

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