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All Journal Bionatura Jurnal Ilmu Ternak Veteriner WARTAZOA Indonesian Bulletin of Animal and Veterinary Sciences Educenter: Jurnal Ilmiah Pendidikan EDUCENTER JURNAL PENDIDIKAN

Simson Tarigan

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Author-ID : 454568

Agriculture, Biological Sciences & Forestry Biochemistry, Genetics & Molecular Biology Economics, Econometrics & Finance Education Health Professions Immunology & microbiology Veterinary

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Ingestion of host immunoglobulin by Sarcoptes scabiei Simson Tarigan
Jurnal Ilmu Ternak dan Veteriner Vol 10, No 1 (2005): MARCH 2005
Publisher : Indonesian Center for Animal Research and Development (ICARD)

Scabies is one of the most important diseases in human and veterinary medicine. The available control measures that rely on acaricides are unsustainable, costly and environmentally unfriendly. Vaccination which is supposedly the most attractive alternative control, is sustainable, potentially cheap and environmentally friendly. Recent development in protein biochemistry and recombinant technology have facilitated the development of anti-parasite vaccine which in the past was impossible. One prerequisite for the anti-parasite-vaccine development is that the parasite has to ingest its host immunoglobulin. This study, therefore, was designed to determine whether Sarcoptes scabiei, a non blood-feeding parasite that resides on the avascular cornified layer of the skin, ingest its host immunoglobulin. Sections of routinely processed mites and skin from a mangy goat were probed with peroxidase-conjugated-anti-goat IgG and the immune complex was visualised with diaminobenzidine solution. To determine whether the ingested IgG was still intact or had been fragmented by the proteolytic enzymes, immunoblotting analysis of SDS-PAGE- fractionated proteins extracted from washed mites was performed. Quantification of IgG was done byan Elisa using purified goat IgG as control. This study showed that IgG in the mites confined to the mite’s gut only, and only a fraction of mite population ingested the IgG. The ingested IgG, as shown by immunoblot analysis, was mostly still intact. This study indicates that development of anti-scabies vaccines is reasonable. Key Words: Sarcoptes scabiei, Immunoglobulin

Identification and characterisation of heat-stable allergens from Sarcoptes scabiei Simson Tarigan
Jurnal Ilmu Ternak dan Veteriner Vol 11, No 1 (2006): MARCH 2006
Publisher : Indonesian Center for Animal Research and Development (ICARD)

Animals or human recovered from Sarcoptes scabiei infestation acquired protective immunity against reinfestation. The protective immunity is considered to be associated with a type-1-hypersensitivity reaction against allergens instigated by the mites during infestation. It is assumed that these allergens have the potential to be used as the main component of an anti-scabies vaccine. The purpose of this study is to identify and characterise the sarcoptic allergens. For this purpose, 645 mg of mites, collected from mangy goats, were homogenised in PBS to prepare soluble mite proteins. Fractionation of proteins was initially performed on a Q-sepharose column but the results were unsatisfactory. Consequently, SDS PAGE was used as an alternative. Proteins from the gel were transferred onto a nitrocellulose membrane. The membrane was cut into strips so each strip contained proteins with molecular weights of ³ 90, 80-90, 70-80, 60-70, 50-60, 40-50, 30-40, 25-30, 20-25, 15-20 and 10-15 kDa, respectively. The heat stability of the allergens was determined by heating the suspension at 60ºC for 60 minutes, whereas their dialysability was evaluated using a 10-kDa-cut-off ultramembrane. The activity of the allergens was assayed by an intradermal test on sensitised goats. This study showed that mite protein extract was very potent allergens since mite extract containing as little as 1 ng mite proteins still caused an obvious hypersensitive reaction. The mite extract contained heat-stable, dialysable and non-dialysable allergens. All fractions recovered from a Q-sepharose column contained allergens with almost equal potency. Fractionation with the SDS-PAGE revealed that the allergens had molecular weights of 35 and <10 kDa. The former allergen is assumed to be a member of group 10 allergens, whereas the later belong to haptenic allergens. Kata Kunci: Sarcoptes Scabiei, Allergens, Heat-Stable, Group 10, Hapten

Actinobacillus pleuropneumoniae cytotoxins on size, granularity and viability of porcine neutrophils Simson Tarigan
Jurnal Ilmu Ternak dan Veteriner Vol 3, No 3 (1998)
Publisher : Indonesian Center for Animal Research and Development (ICARD)

Cytotoxins produced by Actinobacillus pleuropneumoniae are supposed to play major roles in bacterial pathogenicity and virulence. To gain better understanding in the mechanism of the pathogenicity, cytotoxic activities of the toxins on porcine neutrophils were investigated in vitro. Changes in cell size, granularity and viability were examined with a flow cytometer. Cell size and granularity correlate with forward light scatter and right angle light scatter, respectively; whereas, cell viability corresponds with fluorescent intensity of cells stained with propidium iodide . At low concentrations (dilutions between 1/10 and 1/100 of bacterial culture supernatants), the cytotoxins induced severe swelling and degranulation of neutrophils; whereas, at higher concentrations (dilutions of 51/10 bacterial culture supernatants), the cytotoxins caused rapid cell death. There was no significant difference in cytotoxic activities of Cyooxins derived from various serotypes (serotypes 1, 2, 3, 5 and 7 ) of A. pleuropneumoniae . Morphologically, the cytotoxin-treated neutrophils stained with Giemsa showed profound changes. Neutrophils treated with low dosages of Cyooxins became swollen with spherical nuclei . Higher concentration of cytotoxins study indicates strongly that important mechanism in the caused vactiolation of cytoplasts, enlargement or disintegration of nuclei . This in vitro intoxication of neutrophils by cytotoxins produced by A. pleuropneumoniae comprises anpathogenicity of the bacteria. Key words : Actitiobacilluspleuropneumoniae, cytotoxin, neutrophils, pig, flow cytometry

Characterisation of enzymatic activities of H5N1 influenza virus Simson Tarigan; Risa Indriani; Darminto .
Jurnal Ilmu Ternak dan Veteriner Vol 12, No 2 (2007): JUNE 2007
Publisher : Indonesian Center for Animal Research and Development (ICARD)

One of the two glycoproteins projected from the surface of the influenza virus is identified as neuraminidase. This enzyme enables the virus to spread in the host, and therefore it plays vital roles in the viral pathogenicity. From the viewpoint of disease control, neuraminidase is used as the target for the development of anti-flu drugs, and for the development of diagnostic test to differentiate infected from vaccinated animals (DIVA). Since the roles of the enzyme are very important, information regarding the characteristics and the procedure to measure its activity, which is the purpose of this study, is essential. The optimum incubation time of the neuraminidase-substrate (fetuin) reaction and the optimum pH of the buffer were determined. The stability of the enzyme against heating, supplementation or chelating of calcium ion, and b-propiolactone treatment were analysed. This study showed that neuraminidase from H5N1-influenza virus was, in regards to the characteristics investigated in this study, was comparable to that from Clostridium perfringens. The optimum incubation time for the viral and Clostridial neuraminidases were 60 and 30 minutes, respectively; whereas, the optimum pH for both neuraminidase was 6-7. At pH 8, both neuraminidase were inactive. Supplementation of calcium ion tended to increase activity but chelating of the cation did not have any observable effects. Treatment with 0.2% b-propiolactone for 6 hours reduced the activity, whereas heating at 60°C for 60 minutes abolished all activity. Since inactivation by b-propiolactone is partially only, neuraminidase assay could be performed safely in ordinary laboratories using b-propiolactone-treated-influenza virus, rather than the life virus. The thermolabile nature of the enzyme will complicate any attempt to purify the enzyme. Key Words: H5N1, Neuraminidase, Stability, Thiobarbituric Assay

Production and purification of Bacillus anthracis protective antigen Simson Tarigan; Rahmat S Adji; Lily Natalia
Jurnal Ilmu Ternak dan Veteriner Vol 10, No 3 (2005): SEPTEMBER 2005
Publisher : Indonesian Center for Animal Research and Development (ICARD)

Protective antigen (PA) plays crucial roles in the pathogenicity and virulence of Bacillus anthracis. Animals or human immunised with the protein acquire a complete protection against the disease. In addition to vaccine, PA can also be developed into a sensitive diagnostic test for anthrax. The purpose of this study was to produce PA using a culture medium easily obtained, and to develop a simple and effective technique for purification of the protein. To produce PA, B. anthracis Sterne 34F2 strain was first grown on blood agar, then bacterial colonies were suspended and incubated for 2 hours in RPMI-1640 supplemented with NaHCO3 and Tris. Protein components in the culture supernatant were separated consecutively with Phenyl sepharose, Qsepharose and Superdex-200 columns. This order was used in order to simplify and speed up the purification process. The PA contained in the fractions was detected by a dot blot or an ELISA using commercial PA specific antibody. The PA was absorbed strongly by the phenyl sepharose whereas other proteins were absorbed weakly or not absorbed at all. When these PA-containing fractions were loaded into Q-sepharose column, PA was absorbed considerably weaker than contaminated proteins. Although the level of purity obtained from the Q-sepharose column was satisfactory, further separation on Superdex produced an even higher purity. However, on SDS-PAGE analysis, the purified PA was seen as a two-band protein (54.7 and 29.2 kDa) because of nicked proteolysis. On an immunoblot assay, only the 54.7 band was recognised by the PA-specific antibody. Despite the nick proteolysis, the PA purified in this study was considered to retain its biological activities. Key Words: Bacillus anthracis, Protective Antigen, Protein Purification

Co-Authors D Hewajuli Darminto . Iman Hernaman J. Ignjatovic Jagoda Ignjatovic Lily Natalia Lumbantoruan, Jenti R Indriani Rahmat S Adji Risa Indriani Risa Indryani Sumarningsih . . Toto Toharmat

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