Characterization Of Antigenic Proteins Research Articles

Identification the Gene Nucleotide Sequence of Outer Membrane Protein Aeromonas Hydrophilla Bacteria from East Java Local Isolates Using Polimerase Chain Reaction

Aeromoniasis disease or known Ulcer Diseases caused by Aeromonas hydrophila which in fish or shrimp often occurs in some embankment or in the Aquarium can cause sign patches – patches of bleeding can even cause economic loss and death if not promptly treated with treatment that accompanied the good sanitation. This disease affects many farmed freshwater fish in East Java. Previous research has managed to do the characterization of antigenic protein originating from the OMP (outer membrane protein) Aeromonas hydrophilla. Because it is felt necessary to do DNA sequensing encoder protein in question.To achieve these goals then do some exploratory research laboratoric methods, namely: identification of the bacterium Aeromonas hydrophilla fish from suspect infection by PCR, gel electrophoresis and Sequencing of gene fragments of the agarosa OMP A. hydrophilla isolates of East Java. The results obtained from this research is the result of agarosa gel electrophoresis in DNA chromosome Aeromonas hydrophila bacteria cells is carried out at a temperature of annealing 54oC position 400 bp and the results of the sequencing primer that is used produces a sequence of nucleotides is around 355 nucleotides. Key words: Aeromonas hydrophilla, agarosa gel electrophoresis, DNA sequencing

Characterization of Antigenic Proteins from Tritrichomonas foetus Recognized by Antibodies in Rabbit Serum, Bovine serum and Bovine cervicovaginal Mucus

Tritrichomonas foetus is an obligate parasite of the bovine urogenital tract and is recognized as 1 of the more common infectious agents causing decreased reproductive efficiency in beef cattle. Infections result in reproductive failure and produce considerable economic loss. Vaccination of heifers with vaccines containing T. foetus induces elevated serological responses to many T. foetus antigens, decreases the rate and/or length of infection with T. foetus, and decreases fetal loss caused by infection. Because T. foetus infections are usually limited to lumen and mucosal surfaces of the reproductive tract, it has been assumed that protection from infection and abortion is partially mediated by immunoglobulins in the uterus and vagina. The objective of this study was to identify and characterize specific antigens of T. foetus that show promise for use in a recombinant vaccine that will generate a protective mucosal immune response in cattle. Surface proteins were identified by using polyclonal rabbit anti-trichomonal sera eluted from paraformaldehyde-fixed cells. Analyses of these proteins, utilizing mucosal antibodies from vaccinated and convalescent cows, have identified proteins involved in generating a local immune response. Western immunoblot analysis indicates that these proteins are well conserved and are excellent candidates for incorporation into a recombinant vaccine.

Preparation of cell-free extracts from mycobacteria.

AbstractMuch work in the mycobacterial field has focused on the identification and characterization of antigenic proteins (1,2); many have now been identified and assigned a function; for example, the immunodommant 65kDa antigen of Mycobacterzum tuberculosis has been identified as a chaperonin (3) and the 28-kDa antigen of Mycobacterzum leprae was shown to be superoxide dismutase (4). In the beginnings of mycobactertal molecular biology, antigenic proteins were identified by screening M. leprae and M tuberculosis expression libraries in Escherichia coli (5–9) with mouse monoclonal antibodies (MAbs) (7,8) and polyclonal sera from rabbits (10,11) and patients (12,13). Although E. coli is still being used for the overexpression and purification of mycobacterial proteins (14), the use of nonpathogenic mycobacterta, such as Mycobacterium smegmatis as surrogate hosts may be preferable (15). For example, several mycobacterial proteins have been shown to undergo post-translational modification, such as glycosylation (15,16). Because glycosylation does not occur in E. coli, the study of such proteins in their native state requires the use of mycobacterial hosts. The preparation of cell-free extracts and protein purification from mycobacteria is a prerequisite for this kind of work.KeywordsCell DisruptionAntigenic ProteinMycobacterium SmegmatisPolyclonal SeronInsoluble PelletThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Production of monoclonal antibodies against rice dwarf virus and characterization of antigenic proteins with affinity media

Hybridomas were developed which secreted antibodies to the core and outer capsids of rice dwarf virus (RDV). The reactive proteins of RDV were simply and rapidly analyzed using monoclonal antibody (MoAb)-coupled Affi-Gel 701 beads and SDS polyacrylamide gel electrophoresis and were isolated with a MoAb-coupled Sepharose 4B affinity column.