RESUMO
This review paper provides an overview of innovative technologies designed to produce bacterial, viral, recombinant subunit, and polysaccharide vaccines, as well as combination vaccines. Advances in this field are illustrated by vaccines against DTP (diphtheria-tetanus-pertussis), influenza, hepatitis B (HepB) and typhoid fever. In addition, technological trends regarding antigens, adjuvants, and preservatives in vaccines are discussed. The progress achieved in vaccine production technologies is especially important for improving the protection of vulnerable populations against infectious diseases. These at-risk groups include infants, the elderly and immunocompromized individuals, as well as people living in developing countries or emerging economies.
Assuntos
Tecnologia Farmacêutica/métodos , Vacinas/biossíntese , Vacinas/isolamento & purificação , Adjuvantes Imunológicos/química , Animais , Antígenos/biossíntese , Antígenos/isolamento & purificação , Química Farmacêutica , Vacina contra Difteria, Tétano e Coqueluche/biossíntese , Vacina contra Difteria, Tétano e Coqueluche/isolamento & purificação , Vacinas contra Hepatite B/biossíntese , Vacinas contra Hepatite B/isolamento & purificação , Humanos , Vacinas contra Influenza/biossíntese , Vacinas contra Influenza/isolamento & purificação , Polissacarídeos Bacterianos/biossíntese , Polissacarídeos Bacterianos/isolamento & purificação , Conservantes Farmacêuticos/química , Vacinas/imunologia , Vacinas Combinadas/biossíntese , Vacinas Combinadas/isolamento & purificação , Vacinas Sintéticas/biossínteseRESUMO
The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.
Assuntos
Antígenos de Superfície da Hepatite B/biossíntese , Vacinas contra Hepatite B/biossíntese , Pichia/metabolismo , Western Blotting , Dimerização , Eletroforese em Gel de Poliacrilamida , Glicosilação , Antígenos de Superfície da Hepatite B/genética , Vacinas contra Hepatite B/genética , Substâncias Macromoleculares , Pichia/genética , Processamento de Proteína Pós-TraducionalRESUMO
The efficiency of two lypolytic enzymes (fungal cutinase, yeast esterase) in the degradation of dipropyl phthalate (DPrP) was investigated. The DPrP-degradation rate of fungal cutinase was surprisingly high, i.e., almost 70% of the initial DPrP (500 mg/l) was decomposed within 2.5 h and nearly 50% of the degraded DPrP disappeared within the initial 15 min. With the yeast esterase, despite the same concentration, more than 90% of the DPrP remained even after 3 days of treatment. During the enzymatic degradation of DPrP, several DPrP-derived compounds were detected and time-course changes in composition were also monitored. The final chemical composition after 3 days was significantly dependent on the enzyme used. During degradation with fungal cutinase, most DPrP was converted into 1,3-isobenzofurandione (IBF) by diester hydrolysis. However, in the degradation by yeast esterase, propyl methyl phthalate (PrMP) was produced in abundance in addition to IBF. The toxic effects of the final degradation products were investigated using various recombinant bioluminescent bacteria. As a result, the degradation products (including PrMP) from yeast esterase severely caused oxidative stress and damage to protein synthesis in bacterial cells, while in the fungal cutinase processes, DPrP was significantly degraded to non-toxic IBF after the extended period (3 days).
