sepharose and Swine-Diseases

The aim of study was to determine the influence of zinc chelate, valnemulin and it's combination on Brachyspira hyodysenteriae shedding and morphological changes of colonic mucosa in an experimental model of swine dysentery (SD). The study was performed on pigs coming from a dysentery-free herd. Animals were inoculated by B. hyodysenteriae strain B204. When the clinical signs of SD and B. hyodysenteriae shedding developed, the pigs were divided into four treatment groups. The first group was treated with zinc chelate (250 ml/1000 L in water), second group was given valnemulin in feed at 75 ppm; the third group was given a combination of both and the fourth group was control. The results demonstrated therapeutic effect of valnemulin in pigs with serious SD and did not show therapeutic effect of chelated zinc.

Topics: Animals; Brachyspira hyodysenteriae; Colon; Diterpenes; Drug Therapy, Combination; Dysentery; Gram-Negative Bacterial Infections; Immunohistochemistry; Intestinal Mucosa; Sepharose; Swine; Swine Diseases

Adaptation of field isolates of foot-and-mouth disease virus (FMDV) to grow in cells in culture can result in changes in viral properties that include acquisition of the ability to bind to cell surface heparan sulfate (HS). After 13 passages on BHK cells to produce a vaccine, a Cathay topotype isolate of FMDV serotype O from China (O/CHA/90) extended its cell culture host range and bound to heparin-Sepharose, although it did not require cell surface HS as a receptor molecule. To understand these phenomena, we constructed chimeric viruses by using a type A(12) infectious cDNA and the capsid protein-coding regions of O/CHA/90 and its cell culture-adapted derivative (vac-O/CHA/90). Using a set of viruses derived from these chimeras by exchanging portions of the capsid-coding regions, we discovered that a group of amino acid residues that surround the fivefold axis of the icosahedral virion determine host range in cell culture and influence pathogenicity in pigs. These residues included aromatic amino acids at positions 108 and 174 and positively charged residues at positions 83 and 172 in protein 1D. To test if these residues participated in non-integrin-dependent cell binding, the integrin-binding RGD sequence in protein 1D was changed to KGE in two different chimeras. Evaluation of these KGE viruses indicated that growth in cell culture was not dependent on HS. One of these viruses was tested in pigs, where it produced a mild disease and maintained its KGE sequence. These results are discussed in terms of receptor utilization and pathogenesis of this important pathogen.

Topics: Amino Acid Sequence; Animals; Binding Sites; Capsid Proteins; Cell Line; China; Cricetinae; Foot-and-Mouth Disease; Foot-and-Mouth Disease Virus; Genetic Engineering; Heparitin Sulfate; Models, Molecular; Molecular Sequence Data; Oligopeptides; Recombinant Fusion Proteins; Sepharose; Swine; Swine Diseases; Virion

The standardization of pig neutrophil chemotaxis under agarose is described. The mean chemotactic index for pig neutrophils from six pigs measured over four days was 1.29. Comparative studies of human and pig neutrophil chemotaxis under agarose revealed a lower chemotactic index for pig neutrophils (mean of 1.18) compared to human neutrophils (mean of 2.43). The results suggest that this is due to differences intrinsic to human and pig neutrophils. In vitro pig neutrophil chemotaxis was measured in normal pigs and in pigs following experimental Salmonella typhimurium infection. Significant alterations in chemotaxis were not evident one and seven days postinfection.

Topics: Animals; Animals, Newborn; Cell Movement; Chemotaxis, Leukocyte; Humans; Neutrophils; Salmonella Infections, Animal; Salmonella typhimurium; Sepharose; Swine; Swine Diseases

Eleven out of 25 pigs were immunized with a lectin--agarose based subunit vaccine for Aujeszky's disease (AD). The vaccine was prepared by extracting protective antigens from a non-ionic detergent (Triton-X-100) extract of AD virus-infected PK-la cells with Lens culinaris agglutinin immobilized on agarose beads. Two groups of 3 and 4 pigs received 2 doses of vaccine each containing 426 micrograms of adsorbed protein. Two groups of 2 pigs each received 2 vaccine doses containing either 23 or 33 micrograms of adsorbed protein. All vaccinated pigs survived a nasal challenge of 10(8.5) PFU of virulent AD virus while 13 out of 14 (93%) uninoculated controls died between Days 5 and 9 post challenge. This immunizing preparation qualified as a practical subunit vaccine because pigs were protected with relatively small amounts of protective antigen while at the same time remained free of detectable antibody to a complementary diagnostic antigen. This antigen was obtained in relatively pure form from the maintenance medium of virus-infected cells 4 h post-inoculation. In addition both high and low dose vaccinates failed to produce detectable antibody to at least one other antigen complex. The composition of Lens culinaris agglutinin (LCA) and Ricinus communis agglutinin (RCA)-purified AD viral antigen preparations were also compared by crossed immunoelectrophoretic techniques. Both preparations contained two antigen complexes and two individual antigens in common. Each preparation also contained its own unique antigen complex. The RCA purified antigen preparation also contained small quantities of a single antigen that was not detectable in the LCA antigen preparation.

Topics: Adsorption; Animals; Antibodies, Viral; Antigens, Viral; Dose-Response Relationship, Drug; Evaluation Studies as Topic; Herpesvirus 1, Suid; Immunoelectrophoresis, Two-Dimensional; Lectins; Plant Lectins; Pseudorabies; Sepharose; Swine; Swine Diseases; Vaccination; Viral Vaccines