Cell surface immunoglobulin of hamster lymphoid cells

Eidels, Leon; Proia, Richard L.; Streilein, J. Wayne; Hart, David A.

doi:10.1016/0161-5890(79)90115-9

Cited by 22 publications

(25 citation statements)

References 16 publications

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“…Only the third point has been clarified at the molecular level: it is now known Correspondence address: C. Montecucco, Istituto di Patologia Generale, Via Loredan, 16, 35131 Padova, Italy that protein synthesis is blocked by specific ADPribosylation of elongation factor 2 that causes its detachment from ribosomes [6]. Despite numerous studies little is known about DT binding and translocation; an as yet unidentified receptor protein is involved [7] and the toxin-receptor complex is thought to enter a coated pit and then an endosome [8,9]. There is strong evidence that the low pH of the vesicle lumen is sufficient to allow the toxin to translocate its enzymatic activity to the cytoplasm [10].…”

Section: Introductionmentioning

confidence: 99%

Diphtheria toxin and its mutant crm 197 differ in their interaction with lipids

et al. 1987

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The interaction of diphtheria toxin and its enzymatically deficient mutants crm 176 and crm 197 with liposomes has been studied by turbidity measurement and hydrophobic photolabelling with photoactivatable phosphatidylcholines. Diphtheria toxin and crm 176 at neutral pH bind to the surface of lipid bilayers while crm 197 also appears to interact with the fatty acid chains of phospholipids. All proteins undergo a change in conformation over the same range of acidic pH and become able to insert in the lipid bilayer. The tighter lipid interaction of crm 197 may account for its higher cell association constant. The possibility is discussed that the binding of diphtheria toxin to cells is mediated by both a protein receptor and an interaction with the head group of phospholipids. Diphtheria toxin; Toxin mutant; Lipid interaction

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Section: Introductionmentioning

confidence: 99%

Diphtheria toxin and its mutant crm 197 differ in their interaction with lipids

et al. 1987

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“…Gangliosides and carbohydrates existing as glycolipids or glycoproteins on the cell surface have been long implicated as major receptors for biological toxins, as well as for the cell-cell recognition and hormones. 2 Gangliosides contain both hydrophilic and hydrophobic regions and carry negative electric charges. The hydrophobic portion, ceramide, consists of a long-chain fatty acid linked to the amino alcohol sphingosine through the amide bond.…”

Section: Introductionmentioning

confidence: 99%

A Simple and Sensitive Piezoelectric Immunosensor for Cholera Toxin Based on GM1‐Incorporated Liposome Agglutination

Liu

Wang²,

et al. 2010

Chin. J. Chem.

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A sensitive piezoelelctric immunosensor has been developed for the direct detection of cholera toxin. The proposed technique is based on specific interface agglutination of GM1 incorporated liposome vesicles in the presence of the cholera toxin, which causes a frequency change and is monitored by a piezoelectric device. The interface agglutination reaction would take place as soon as the cholera toxin (CT) was captured by the antibodies modified on the probe surface and the GM1 incorporated liposome in the probe cell. Meanwhile, the agglutination reaction induced both the mass effect and viscoelastic effect acting on the probe surface. The results indicate that the probe signal can be observably multiplied. In addition, an optimization of liposome composition and assay medium were investigated. Moreover, no cross-reactivates were observed with the common protein, such as goat anti-mouse IgG (1 mg/mL), mouse IgG (1 mg/mL), goat anti-human IgG (1 mg/mL), and thrombin (1 mg/mL). The frequency responses of the developed piezoelelctric immunosensor are linearly correlated to cholera toxin concentration in the range of 0.5 to 7.5 µg/mL with a detection limit of 0.27 µg/mL while showed no significant loss in activity over 3 d under storage at 4 ℃.

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“…Upon penetration of the cell membrane, the A subunits cause irreversible activation of adenylate cyclase by NAD-dependent ADPribosylation of the GTP-binding component of the cyclase, and the resulting electrolyte imbalance causes massive fluid loss into the lumen of the intestine. A subunits alone are not capable of penetrating the target cells and the B subunits alone possess n o toxin activity [4,5).…”

mentioning

confidence: 99%

Inactivation of the Escherichia coli heat‐labile enterotoxin by in vitro mutagenesis of the A‐subunit gene

Harford¹,

Dykes

Hobden

et al. 1989

European Journal of Biochemistry

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In vitro mutagenesis of the LTA gene, encoding the A subunit of the Escherichia coli heat‐labile enterotoxin, has been used to obtain A subunits deficient in enzymic activity. One inactive A‐subunit mutant which contained two amino acid substitutions, was shown to associate with native B subunits to form a holotoxoid lacking toxin activity. A serine to phenylalanine mutation appears to be responsible for the loss of toxicity.

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Cell surface immunoglobulin of hamster lymphoid cells

Cited by 22 publications

References 16 publications

Diphtheria toxin and its mutant crm 197 differ in their interaction with lipids

Diphtheria toxin and its mutant crm 197 differ in their interaction with lipids

A Simple and Sensitive Piezoelectric Immunosensor for Cholera Toxin Based on GM1‐Incorporated Liposome Agglutination

Inactivation of the Escherichia coli heat‐labile enterotoxin by in vitro mutagenesis of the A‐subunit gene

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