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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Escherichia coli bacteriophage T4 uses the lipopolysaccharide of the outer cell envelope membrane as a receptor. Lipopolysaccharide from E. coli K-12 required a major outer membrane protein, polypeptide Ib, for phage inactivation.
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PMID:Two-component nature of bacteriophage T4 receptor activity in Escherichia coli K-12. 36 36

The outer membranes of the smooth Proteus mirabilis S1959 strain and its rough R13, R110, R51 and R45 mutants were isolated by sonication of the cells and sucrose density gradient centrifugation. The outer membrane of the rough strains had a lower density than that of their parent smooth strain, but the protein-to-phospholipid ratios were the same. The electrophoretic patterns of outer membrane polypeptides of the S and R strains in sodium dodecylsulfate/polyacrylamide gels were identical, with two major polypeptide bands, C1 and C2 (Mr 39,000 and 38,000) predominating. The C1 polypeptide band was a heat-modifiable polypeptide, which migrated as a band at Mr 33,000 when membranes were solubilized at 37 degrees C or 50 degrees C, and at Mr 39,000 when solubilization was at 100 degrees C. Susceptibility of outer membrane polypeptides to proteolytic digestion was found to be higher in isolated outer membrane preparations of the rough strains than in the smooth strain, suggesting that the availability of the polypeptide chains to proteolytic activity depends on the length of the polysaccharide chains of the outer membrane lipopolysaccharide.
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PMID:Outer membrane proteins of smooth and rough strains of Proteus mirabilis. 38 81

The enhanced solubility of hexadecane in the growth medium of hexadecane-grown Acinetobacter species has been related to the accumulation of an extracellular vesicular component. The partition of hexadecane was determined by measuring the amount of [3H]hexadecane bound to the vesicular particle. The vesicle was characterized as a phospholipid-rich, lipopolysaccharide-rich particle with a polypeptide composition similar to the outer membrane of Acinetobacter. The accumulation of an extracellular vesicular component that binds hexadecane in the form of a microemulsion represents another example of molecules produced by microorganisms in response to paraffinic substrates.
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PMID:Partition of alkane by an extracellular vesicle derived from hexadecane-grown Acinetobacter. 50 May 68

The atypical Bacteroides fragilis lipopolysaccharide is chemotactic for polymorphonuclear leukocytes. The chemotactic activity is mediated by complement activated through the alternative pathway. This mediator has been isolated. It is a polypeptide with a molecular weight of 16,000 and is most likely the complement component C5a.
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PMID:The chemotactic effect of Bacteroides fragilis lipopolysaccharide. 54 86

The adsorption apparatus of phage 2 consits of a symmetrical base plate of snowflake appearance, composed of six droplike spikes 7.0 to 7.5 nm in length with a maximum diameter of 4.5 to 5.0 nm. The spikes are attached by their narrow ends to a central ring 7.0 to 7.5 nm in diameter. Phage 2 deopolymerase, a phage 2-induced hydrolytic enzyme, was found to be a structural protein of phage 2 or in close association with the base plate. Pdp1, a phage 2 mutant, possesses a polypeptide that is antigenically similar to the depolymerase, but devoid of hydrolytic activity. This polypeptide was found to be located in the region of the base plate of pdp1. Treatment of intact cells of strain BI with purified phage 2 depolymerase inhibited the adsorption of phage 2. When phage receptor-containing fractions of slime glycolipoprotein and lipopolysaccharide were hydrolyzed by the depolymerase, amino sugars were released, and the phage-inactivating activities of these fractions were lost. The depolymerase was also observed to induce the lysis of strain BI cells in hypotenic medium. The phage 2 depolymerase appears to play a role in adsorption and release of phage.
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PMID:Localization and functional role of the pseudomonas bacteriophage 2 depolymerase. 81 8

Cell envelopes of Haemophilus influenzae have been prepared by breakage in a French pressure cell followed by differential centrifugation. The envelope fraction may be resolved into an inner-membrane (light) and an outer-membrane (heavy) fraction on density gradients. Envelopes from competent cells possess elevated levels of lipopolysaccharide with a composition different from that of log-phase cell envelopes. Three apparently new polypeptides have been observed in envelopes from competent cells by gel electrophoresis in sodium dodecyl sulfate; additional quantitative alterations in the profiles of membrane polypeptides also company the development of the capacity to transport deoxyribonucleic acid. Most of the polypeptide changes are confined to the outer membrane; one new polypeptide is associated with the inner cytoplasmic membrane of competent cells. Protein synthesis during competence developement is rquired for the change in lipopolysaccharides and in the envelope polypeptides to occur.
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PMID:Constitution of the cell envelope of Haemophilus influenzae in relation to competence for genetic transformation. 108 Apr 85

The in vivo adjuvant effect of lipopolysaccharide (LPS) in mice was investigated with the soluble synthetic polypeptide antigen (T, G)-A--L, the antibody response to which is determined by the Ir-1A gene. With this specific antigen it can be demonstrated that the LPS adjuvant effect has the following modes of action: a) a T cell-dependent enhancement of primary and secondary IgM antibody response; b) a T cell-dependent enhancement of IgG secondary andibody response; and c) a T cell-dependent induction of switchover from IgM to IgG andibody in some strains of Ir-1A low responders. Although T cells are necessary for some aspects of the adjuvant effect, these data do not distinguish between a mechanism involving a direct interaction between LPS and T cells or a direct interaction of LPS and B cells with a general requirement for T cells for expression of IgG antibody.
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PMID:T cell requirements for the expression of the lipopolysaccharide adjuvant effect in vivo: evidence for a T cell-dependent and a T cell-independent mode of action. 108 42

1. The crude envelope preparation obtained by sonication of Proteus mirabilis cells in the presence of lysozyme was separated into outer and cytoplasmic membrane fractions by sucrose density gradient centrifugation. The outer membrane fraction accounted for about two thirds of the dry weight of the envelope preparation. 2. In thin sections, the outer and cytoplasmic membrane fractions were shown to consist of vesicles bounded by a single trilaminar membrane, but those of the outer membrane were considerably smaller and were frequently open, forming C-shaped structures. The cytoplasmic membrane vesicles were cleaved by freeze fracturing to expose fracture faces studded with particles, while the outer membrane fragments resisted cleavage. 3. The outer membrane fraction consisted of protein (similar to 40%), lipopolysaccharide (similar to 36%) and lipid (similar to 18%) and had a density of about 1.22 g/cm3. The cytoplasmic membrane fraction consisted mostly of protein (similar to 56%) and lipid (similar to 38%), had a density of about 1.16 g/cm3, and contained almost all the NADH oxidase, succinate and D-lactate dehydrogenase activities of the crude envelope preparation. 4. Electrophoresis in polyacrylamide gels containing sodium dodecylsulfate revealed over 20 polypeptide bands in the cytoplasmic membrane fraction and only 6-7 in the outer membrane fraction. The outer membrane electrophorogram was dominated by a major band (mol. wt 40 000) which was resolved into two bands when electrophoresed in an acidic gel system. Amino acid analysis revealed a higher content of polar amino acids in the protein moiety of the outer membrane.
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PMID:The outer membrane of Proteus mirabilis. I. Isolation and characterization of the outer and cytoplasmic membrane fractions. 109 Dec 89

Protein II*, one of the major Escherichia coli outer cell envelope membrane proteins has been characterized. The protein is heat-modifiable and perhaps due to complete unfolding and/or binding of sodium dodecylsulfate only at higher temperatures the modified protein exhibits a higher apparent molecular weight (33,000) than the non-modified form (28,000). Protein-chemical evidence as well as the behavior of two mutant proteins II* very strongly suggest that this protein consists of a single polypeptide chain and that in the strains studied there is no other major protein with similar characteristics. For another outer membrane protein, protein III (molecular weight 17,000), it has not yet been established if it should be classified as a major protein. Protein III consists of one or perhaps two polypeptide chains. The possibility existed that protein III is bound covalently to lipopolysaccharide, and this has been ruled out. Also, the lipopolysaccharide of the E. coli strains studied does not carry covalently bound protein in amounts anywhere near stoichiometry. N-on-protein substituents were neither found in protein II* nor in protein III. It is concluded that in E. coli B/r and the E. coli K12 strains used there are three major proteins: I, II, and IV; protein III may also belong to this class. There are not more major proteins than these. All four proteins are compared and discussed regarding their unknown functions and their relation to E. coli outer membrane proteins studied by other authors.
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PMID:The major proteins of the Escherichia coli outer cell envelope membrane. Characterization of proteins II* and III, comparison of all proteins. 110 24

Envelope proteins of one smooth (S) strain and seven rough (R) mutants of Salmonella minnesota were examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. All strains gave similar band patterns although some consistent differences were detected. A major polypeptide band at 54k, which coincided with the flagellar component, was more prominent in S, Ra and Rb than in the Rc, Rd and Re chemotypes. The latter strains, however, showed more prominent bands at 48, 19 and 18k. The stage of growth at which the cultures were harvested was also found to affect the band patterns, particularly in the 54 and 40k regions. A closer examination of S, Ra and Re strains suggested that the levels of the major 40 and 37k bands were slightly reduced in Re. It is concluded that the progressive loss of lipopolysaccharide components which occurs from the S chemotype through various degrees of roughness to Re is accompanied by a change in the envelope protein composition, apparently between Rb and Rc.
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PMID:Envelope proteins in Salmonella minnesota mutants. 115 43


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