Preparation and Properties of a Freeze-dried B.C.G. Vaccine of Increased Stability

Ungar, J.; Muggleton, P. W.; Dudley, Joel; Griffiths, Margaret I.

doi:10.1136/bmj.2.5312.1086

Cited by 31 publications

(5 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…microti OV254 is maintained at the National Institute for Medical Research on Lo$ wenstein-Jensen slopes. Cells were grown up at 37 mC in Tween2\glutamate medium (' glycerol-free medium ' [7], modified from the glycerol-free medium of [8]), 3 litres in 5 litre conical flasks, stirred with a magnetic stirrer bar. After 4 to 5 days, when the attenuance at 450 nm had reached 0.7-0.9, the cells were harvested by centrifugation at 16 000 g for 5 min, washed once with Tris\Tween2 [0.1 M Tris\HCl (pH 7.2)\0.1 % Tween2-80], and resuspended in approx.…”

Section: Strains and Culture Conditionsmentioning

confidence: 99%

Galactosamine in walls of slow-growing mycobacteria

Draper¹,

Khoo

Chatterjee

et al. 1997

Biochemical Journal

View full text Add to dashboard Cite

Galactosamine was found consistently as a minor component of the envelope of five species of slow-growing mycobacteria, including all the major human pathogens, but not three rapid-growing species. The amino sugar was a component of the arabinogalactan of the cell wall skeleton, and occurred at the level of about one residue per arabinogalactan chain. Its amino group was in the free, un-N-acetylated state. Examination of oligosaccharides released by partial acid hydrolysis of arabinogalactan by fast atom bombardment-MS and gas chromatography-MS identified a series of oligoarabinans, each possessing one GalN unit, linked to position 2 of arabinose. It is proposed that the GalN residues occur as stub branches of 1-->5-linked arabinose chains in the arabinogalactan. Possible functions of GalN are discussed.

show abstract

Section: Strains and Culture Conditionsmentioning

confidence: 99%

Galactosamine in walls of slow-growing mycobacteria

Draper¹,

Khoo

Chatterjee

et al. 1997

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…Lyophilization is used to stabilize therapeutic proteins [13] and potentially may extend the shelf life and thermostability of vaccines as well [14,15,16]. In the design of a lyophilized vaccine formulation, a primary objective is to use judiciously-chosen excipients [13] to embed the antigen in a glass whose high viscosity and low water content limit degradation reactions.…”

Section: Introductionmentioning

confidence: 99%

Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization

Hassett

Cousins

Rabia

et al. 2013

European Journal of Pharmaceutics and Biopharmaceutics

View full text Add to dashboard Cite

Lyophilization was used to prepare dry, glassy solid vaccine formulations of recombinant ricin toxin A-chain containing suspensions of colloidal aluminum hydroxide adjuvant. Four lyophilized formulations were prepared by using combinations of rapid or slow cooling during lyophilization and one of two buffers, histidine or ammonium acetate. Trehalose was used as the stabilizing excipient. Aggregation of the colloidal aluminum hydroxide suspension was reduced in formulations processed with a rapid cooling rate. Aluminum hydroxide particle size distributions, glass transition temperatures, water contents, and immunogenicities of lyophilized vaccines were independent of incubation time at 40°C for up to 15 weeks. Mice immunized with reconstituted ricin toxin subunit A (RTA) vaccines produced RTA-specific antibodies and toxin-neutralizing antibodies (TNA) regardless of the length of high temperature vaccine storage or the degree of aluminum adjuvant aggregation that occurred during lyophilization. In murine studies, lyophilized formulations of vaccines conferred protection against exposure to lethal doses of ricin, even after the lyophilized formulations had been stored at 40°C for 4 weeks. A corresponding liquid formulation of vaccine stored at 40°C elicited RTA-specific antibody titers but failed to confer immunity during a ricin challenge.

show abstract

“…Mycobacterium bovis BCG (Glaxo strain) was a gift from Glaxo Laboratories Ltd., Greenford, Middlesex, England. The organisms were grown in glycerol-free medium (30) and supplied as a suspension containing 150 mg (wet weight) of organisms per ml. This suspension 30 was counted by the method of Hart and Rees (7) and contained 0.9 x 10" organisms per ml.…”

mentioning

confidence: 99%

Activation of the alternative pathway of complement by mycobacteria and cord factor

Ramanathan¹,

Curtis²,

Turk³

1980

Infect Immun

View full text Add to dashboard Cite

The ability of a number of mycobacteria and some of their components to activate complement was examined. Mycobacterium bovis BCG (Glaxo strain), Mycobacterium leprae, Mycobacterium lepraemurium, and cord factor activated the alternative pathway of complement in normal human serum and normal and C4-deficient guinea pig sera and generated biologically active products. BCG (Pasteur strain) and muramyl dipeptide did not activate complement. The relevance of activation of complement by mycobacteria to their induction of granulomas is discussed.

show abstract

Preparation and Properties of a Freeze-dried B.C.G. Vaccine of Increased Stability

Cited by 31 publications

References 4 publications

Galactosamine in walls of slow-growing mycobacteria

Galactosamine in walls of slow-growing mycobacteria

Stabilization of a recombinant ricin toxin A subunit vaccine through lyophilization

Activation of the alternative pathway of complement by mycobacteria and cord factor

Contact Info

Product

Resources

About