The requirements for insulin presentation and recognition by A alpha b A beta b- and A alpha b A beta k-restricted mouse T cells were studied using a variety of derivatives of the insulin A chain. It was found that A chain peptides with irreversibly blocked Cys residues are non-stimulatory for the T cells. This suggests that at least one of the Cys residues is essential for recognition. On the other hand, all A chain peptides containing Cys residues modified in a way reversible by reaction with thiols are stimulatory yet differ in antigenic potency. All these A chain derivatives including a 14 amino acid fragment require uptake by antigen presenting cells (APC) for efficient presentation. Differences in stimulatory potency between the A chain peptides derived from the same insulin appear to be mainly due to the efficiency of uptake and/or processing by APC. Based on these findings we propose that processing in the case of insulin and its A chain derivatives involves the reductive deblocking of Cys residues or the rearrangement of disulfide bonds apart from a possible proteolytic cleavage. The same may apply to other proteins if Cys residues in the presented peptides are important for the interaction with Ia or the T cell receptor.

Animals↗

PubMedDate not supplied

Protein loss in piglets infected with different enteropathogenic types of Escherichia coli.

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Albumins↗

PubMedDate not supplied

Branched oligoester microspheres fabricated by a rapid emulsion solvent extraction method.

Methyl formate was used as the solvent of biodegradable oligoesters for the fabrication of microspheres with encapsulated bovine serum albumin (BSA). The procedure of dispersion of the double emulsion of the w/o/w type and its dilution and solvent extraction is very rapid, taking only several minutes. A higher yield and better encapsulation efficiency were obtained with copolymers of DL-lactic acid with mannitol than with pure linear poly DL-lactic acid. The procedure was accelerated, and yields and encapsulation efficacy were enhanced by the addition of 5% methyl formate to the external water phase. The microspheres were smaller than 100 microm. No benefits were obtained from the addition of wetting agents or other additives to the intermediate (oligoesteric) phase. Further development should concentrate particularly on hydrodynamic conditions and optimization of the composition of the external phase.

Animals↗

PubMedDate not supplied

Antigenic and adjuvant activities of branched aliphatic oligoester (M-DL-LA) microspheres with incorporated bovine rotavirus.

Branched aliphatic oligoester microspheres (msp) with incorporated rotavirus were used to induce the production of systemic and mucosal antibodies in mice. The msp with a mean diameter of 7.4 microm were prepared by the w/o/w technique. The mice were immunized intraperitoneally or orally. High ELISA titres of systemic and local IgG and IgA antibodies were indicative of rotavirus incorporation and of the adjuvant activity of msp. Oral immunization with a split dose administered on three consecutive days, resulted in the production of systemic IgG and IgA antibodies, but failed to induce the production of mucosal antibodies even if the immunization dose was increased threefold. Specific antibodies were detectable in faeces of orally immunized mice only after another triple administration of the same dose in the fourth week of the experiment. Reactions of blood serum IgG with the structural viral proteins VP4, VP6, and VP7 were demonstrated by western blotting. Both systemic, and faecal IgA antibodies were specific for the VP6 protein and the dimeric form of the glycoprotein VP4.

Adjuvants, Immunologic↗