Anti-schistosomal activity of colostral and mature camel milk on Schistosoma mansoni infected mice. (57/284)

The aim of the present study was to investigate the anti-schistosomal activity of colostral and mature camel milk on Schistosoma mansoni infected mice. Six weeks post infection, mean percentage of protection was detected through the hepatic portal vein. Glutathione-s-transferase (GST), alanine, aspartate transaminase (ALT and AST) and immunoglobulin G (IgG) levels were detected in sera of treated mice before and after infection. Antischistosomal activity of colostral and mature camel milk on Schistosoma mansoni infected mice were 12.81% and 31.60% respectively. The results showed that GST levels in sera of mice fed on colostral and mature camel milk were increased with mean values of 0.070, 0.108, 0.128 and 0.120 in colostral milk groups and 0. 072, 0.085, 0.166 and 0.20 in mature camel milk groups compared with the mice fed on basal diet with means values of 0.070, 0.085, 0.078 and 0.069 before infection and after two, four and six weeks of infection, respectively. On the other hand, there were slight differences on ALT and AST activities. Mice treated with colostral and mature milk (200 microl/day) showed an immunostimulatory effect by inducing IgG titers against soluble worm antigen preparation (SWAP) compared with control. Nevertheless, the difference was not considered significant (0.31 +/- 0.1) for colostrum (0.34 +/- 0.1) and for mature milk, as compared to normal control (0.2 +/- 0.04). Two, four and six weeks post infection, IgG level showed no significant change in sera from mice treated with colostral and mature milk as compared to control. In conclusion, colostral and mature camel milk showed an immuno-modualatory effect in normal healthy mice by inducing IgG and GST levels before and after infection with Schistosoma mansoni. Colostral and mature camel milk have a protective response against schistosomiasis.  (+info)

Camel milk for food allergies in children. (58/284)

BACKGROUND: Food allergies in children are often very serious and can lead to anaphylactic reactions. Observations that camel milk ameliorates allergic reactions were noted over the years. The effect of camel milk is probably related to its special composition. OBJECTIVES: To investigate the effect of camel milk in several children with severe food (mainly milk) allergies. METHODS: We studied eight children with food allergies who did not benefit from conventional treatment. Their parents, or their physicians, decided to try camel milk as a last resort. The parents were advised by the authors - who have considerable experience with the use of camel milk - regarding how much and when the children should drink the milk. The parents reported daily on the progress of their children. RESULTS: All eight children in this study reacted well to the milk and recovered fully from their allergies. CONCLUSIONS: These encouraging results should be validated by large-scale clinical trials.  (+info)

A tandem gene duplication followed by recruitment of a retrotransposon created the paralogous bucentaur gene (bcntp97) in the ancestral ruminant. (59/284)

Retrotransposable element-1 (RTE-1) is a class of long interspersed nucleotide elements that contain in its open reading frame an apurinic/apyrimidinic endonuclease domain (AP-END) and a reverse transcriptase domain. Ruminants have a clade-specific RTE-1 (BovB/RTE). The bovine bcnt gene (bucentaur or craniofacial developmental protein 1) has a duplicated paralog (bcntp97) in tandem that recruited an AP-END of BovB/RTE as a coding exon (RTE exon). We obtained sequence of the bcnt region from several animals and showed that other ruminants also have the bcntp97 with a conserved RTE exon while camels and pigs do not. Genomic Southern analysis showed that camels and pigs have multiple bcnt-related sequences but not BovB/RTE which bovines and lesser mouse deer have abundantly. These results indicate that the bcnt gene duplication followed by the creation of bcntp97 including recruitment of the RTE exon occurred in the ancestral ruminant about 55 MYA. The indication of time frame is supported by a phylogenetic analysis. Taken together with a result of differential tissue expression of the two bcnt paralogs, we conclude that bcntp97 was created concurrently with the early radiation of BovB/RTE in an ancestral ruminant and then acquired a novel function.  (+info)

Grain founder in a male camel (Camelus dromedarius). (60/284)

A rare case of laminitis was recorded in an adult camel that was kept in confinement without giving any exercise and fed daily with considerable quantity of pearl millet grains (Pennisetum typhoideus) for more than five months.  (+info)

Response of camels to intradermal inoculation with smallpox and camelpox viruses. (61/284)

Young camels were inoculated intradermally with either camelpox or smallpox virus and the courses of infection, including serological response, were compared. Camelpox virus was highly infectious; generalized disease resulted which was transmitted naturally to contact animals. Smallpox virus produced only transient lesions at the inoculation site and a less marked serological response. Nevertheless, the camels inoculated with smallpox virus subsequently resisted a severe challenge with camelpox virus, and the possibility that limited replication of smallpox virus took place is discussed. The differences demonstrated between the behavior of the vituses is discussed in the light of their otherwise close relationship and the limited information available about camelpox infections in man.  (+info)

The superior colliculus of the camel: a neuronal-specific nuclear protein (NeuN) and neuropeptide study. (62/284)

In this study we examined the superior colliculus of the midbrain of the one-humped (dromedary) camel, Camelus dromedarius, using Nissl staining and anti-neuronal-specific nuclear protein (NeuN) immunohistochemistry for total neuronal population as well as for the enkephalins, somatostatin (SOM) and substance P (SP). It was found that, unlike in most mammals, the superior colliculus is much larger than the inferior colliculus. The superior colliculus is concerned with visual reflexes and the co-ordination of head, neck and eye movements, which are certainly of importance to this animal with large eyes, head and neck, and apparently good vision. The basic neuronal architecture and lamination of the superior colliculus are similar to that in other mammals. However, we describe for the first time an unusually large content of neurons in the superior colliculus with strong immunoreactivity for met-enkephalin, an endogenous opioid. We classified the majority of these neurons as small (perimeters of 40-50 microm), and localized diffusely throughout the superficial grey and stratum opticum. In addition, large pyramidal-like neurons with perimeters of 100 microm and above were present in the intermediate grey layer. Large unipolar cells were located immediately dorsal to the deep grey layer. By contrast, small neurons (perimeters of 40-50 microm) immunopositive to SOM and SP were located exclusively in the superficial grey layer. We propose that this system may be associated with a pain-inhibiting pathway that has been described from the periaqueductal grey matter, juxtaposing the deep layers of the superior colliculus, to the lower brainstem and spinal cord. Such pain inhibition could be important in relation to the camel's life in the harsh environment of its native deserts, often living in very high temperatures with no shade and a diet consisting largely of thorny branches.  (+info)

High-resolution diffraction from crystals of a membrane-protein complex: bacterial outer membrane protein OmpC complexed with the antibacterial eukaryotic protein lactoferrin. (63/284)

Crystals of the complex formed between the outer membrane protein OmpC from Escherichia coli and the eukaryotic antibacterial protein lactoferrin from Camelus dromedarius (camel) have been obtained using a detergent environment. Initial data processing suggests that the crystals belong to the hexagonal space group P6, with unit-cell parameters a = b = 116.3, c = 152.4 A, alpha = beta = 90, gamma = 120 degrees. This indicated a Matthews coefficient (VM) of 3.3 A3 Da(-1), corresponding to a possible molecular complex involving four molecules of lactoferrin and two porin trimers in the unit cell (4832 amino acids; 533.8 kDa) with 63% solvent content. A complete set of diffraction data was collected to 3 A resolution at 100 K. Structure determination by molecular replacement is in progress. Structural study of this first surface-exposed membrane-protein complex with an antibacterial protein will provide insights into the mechanism of action of OmpC as well as lactoferrin.  (+info)

Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies. (64/284)

Clefts on protein surfaces are avoided by antigen-combining sites of conventional antibodies, in contrast to heavy-chain antibodies (HCAbs) of camelids that seem to be attracted by enzymes' substrate pockets. The explanation for this pronounced preference of HCAbs was investigated. Eight single domain antigen-binding fragments of HCAbs (VHH) with nanomolar affinities for lysozyme were isolated from three immunized dromedaries. Six of eight VHHs compete with small lysozyme inhibitors. This ratio of active site binders is also found within the VHH pool derived from polyclonal HCAbs purified from the serum of the immunized dromedary. The crystal structures of six VHHs in complex with lysozyme and their interaction surfaces were compared to those of conventional antibodies with the same antigen. The interface sizes of VHH and conventional antibodies to lysozyme are very similar as well as the number and chemical nature of the contacts. The main difference comes from the compact prolate shape of VHH that presents a large convex paratope, predominantly formed by the H3 loop and interacting, although with different structures, into the concave lysozyme substrate-binding pocket. Therefore, a single domain antigen-combining site has a clear structural advantage over a conventional dimeric format for targeting clefts on antigenic surfaces.  (+info)