Public health aspects of cystic echinococcosis in the Arab countries.

Human cystic echinococcosis (CE) caused by larval Echinococcus granulosus is a zoonosis of major public health importance throughout the region comprising Arab North Africa and the Middle East. Prevalence rates are determined by epizootiological factors related to the size of stray dog population and its worm burden and to the infection rates in the intermediate host reservoir livestock population. Socio-economic development and socio-cultural practices are considered important determinants in the continued transmission of the disease.

Gestational and neonatal toxoplasmosis: regional seroprevalence in the United Arab Emirates.

Paired maternal/cord blood samples were tested for anti-Toxoplasma IgG or IgM antibodies using Biomerieux Micro-EIA2 IgG and IgM test kits. Of the 1503 women tested at the time of delivery, 344 (22.9%) were IgG seropositive.

Suppression of transplant immunity in experimental trichinellosis.

Skin allograft rejection in Balb/c and C57BL/6J mice following experimental infection with 300 larvae of Trichinella spiralis or Trichinella pseudospiralis was studied. Skin grafts from normal C57BL/6J mice were transplanted to infected Balb/c mice and vice versa at days 3, 10, 20 and 30 post-infection. The clinical criteria for graft rejection, scarring and graft falling, were followed.

Characterization of a synthetic peptide mimicking trypsin-cleavage site of rotavirus VP4.

A synthetic peptide corresponding to the trypsin cleavage site on the 84 k protein of bovine rotavirus was synthesized (VP4-peptide). This synthetic peptide could be cleaved by trypsin and therefore possessed the enzyme binding site present on the authentic protein. Further proof that this peptide mimicks the authentic trypsin cleavage site was the specific reaction of anti-peptide serum with the 84 k protein.

Priming and induction of anti-rotavirus antibody response by synthetic peptides derived from VP7 and VP4.

Synthetic peptides derived from bovine rotavirus C-486 (BRV) outer capsid (VP7 and VP4) and inner capsid (VP6) proteins were tested to evaluate their ability to prime and induce an anti-rotavirus antibody response. Peptides corresponding to the amino acid residues 232-255 of VP4 (VP4-peptide), 275-295 of VP7 (VP7-peptide) and 40-60 of VP6 (VP6-peptide) of BRV were chemically synthesized. These peptides were coupled to carrier proteins (either keyhole limpet haemocyanin (KLH) or recombinant rotavirus inner capsid protein-VP6 assembled into virus-like particles (VP6-carrier) were used as carrier to link the synthetic peptides under study), and the resulting conjugates were used to immunize rotavirus seronegative mice.