HTLV-III gag protein is processed in yeast cells by the virus pol-protease

The gag-pol gene of HTLV-III (human T-lymphotropic virus), the virus linked to AIDS (acquired immune deficiency syndrome), was expressed in yeast, and processing of the gag precursor into proteins of the same size as those in the virion was observed. Processing of the gag gene in yeast cells mimics the process that naturally occurs in mammalian cells during maturation of virions. Therefore it was possible to perform mutational analysis of the virus genome to localize the gene that codes for the protease function to the amino terminal coding region of the pol gene. Since this region overlaps the gag gene, it is likely that ribosomal frameshifting occurs from gag to pol. Antibodies in all of the AIDS patients' sera tested recognized the yeast synthesized gag proteins, although the sera showed differences in relative reactivity to the individual gag proteins and the precursor. This yeast system should be valuable not only for production of viral proteins for diagnostic or vaccine purposes but also for analysis of the genetics and biochemistry of viral gene functions--parameters that are difficult to study otherwise with this virus.     

Iron and transferrin in acute experimental Salmonella cholerae-suis infection in pigs

The effects of experimental Salmonella cholerae-suis inoculation with a virulent and an avirulent strain on serum iron (SI), total iron-binding capacity (TIBC), and transferrin (TF) were evaluated. Inoculation of virulent strain 38 was followed by significant (P less than 0.05) decreases of SI, TIBC, and TF. Exposure to avirulent strain 33 was followed by moderate decreases of SI, TIBC, and TF. When exposure to avirulent strain 33 was followed by challenge exposure with virulent strain 38, the SI, TIBC, and TF values remained at initial values or were higher. Negative correlation was observed between rectal temperature and SI and TIBC values, but was significant (P less than 0.0001) only 7 days after inoculation of the virulent strain 38.     

Failure of passive transfer in foals: incidence and outcome on four studs in New South Wales

Objective To determine the regional incidence and effectiveness of treatment of failure of passive transfer (FPT) in foals. Design A study of disease incidence. Animals Eighty-eight foals and 57 mares from four studs in the practice area of the Rural Veterinary Centre were tested. Procedure Foals were tested for their serum IgG and total serum protein (TSP) concentration within the first 72 hours of life. Colostrum was collected from mares and specific gravity determined. FPT and partial failure of passive transfer (PFPT) of immunoglobulins was diagnosed when serum IgG concentrations were < 4 g/L and 4 to 8 g/L respectively. Owners of foals diagnosed with FPT were offered treatment with 1 to 2 L plasma (TSP > 70 g/L); 9 (64%) of the affected foals were treated. Results Fourteen foals (16%) had FPT whereas 15 (17%) had PFPT. There were significant differences between the mean TSP concentration in foals with FPT (42.6 ± 4.2 g/L), PFPT (48.1 ± 3.9 g/L) and those acquiring adequate passive immunity (58.9 ± 5.5 g/L) (P < 0.01). Sixteen (29%) mares had pre-suck colostral specific gravity < 1.060 and 12 (71%) foals raised by these mares had FPT or PFPT. The incidence of severe disease (categorised by a sepsis score > 11, positive culture of bacteria from blood or disease requiring hospitalisation) in all foals in the first 2 months of life was 10%. However, none of the nine foals with FPT that received plasma experienced severe disease. In contrast, foals with PFPT had an increased susceptibility to severe disease (P < 0.001) when compared with normal foals. Conclusion Treatment of foals with FPT may reduce the subsequent incidence of severe disease. Pre-suck colostral specific gravity and foal TSP may be used to predict the likelihood of FPT and PFPT. Even though the number of foals studied is small the results highlight the importance of optimal management practices in reducing the incidence of FPT and disease associated with this process.     

Immunolocalization of Aquaporins 1 and 9 in the Ram Efferent Ducts and Epididymis

Aquaporins (AQPs) are essential membrane protein channels for the transport of water across membranes. Fluid movement in the epididymis is important for modulation of the luminal environment, in which sperm mature and reside. This study was designed to understand the morphology and localization of AQPs in ram efferent ducts (ED) and epididymis. For this purpose, the epididymis of seven animals were removed for histologic and immunohistochemical analyses. AQP1 immunoreactivity was observed in the apex of the ED, and AQP9 was found adjacent to the nuclei of the epithelial cells of the ED. The epithelial lining of ram epididymis is pseudostratified columnar and presents principal, basal, apical and narrow cells. In the initial segment (IS), a moderate reaction for AQP1 was observed in the apical cytoplasm of epithelial cells. An intense reactivity for AQP1 was noted over the microvilli of principal cells and in spermatozoa in the caput. In the corpus and cauda, AQP1 was noted only over the endothelial cells of vascular channels located in intertubular spaces. A weak‐to‐moderate reaction for AQP9 was observed in the nuclei of epithelial cells in the IS, caput and corpus of the epididymis. In the cauda, an intense reaction to AQP9 was observed in the epithelial border. In the IS, caput and corpus, the reactivity for AQP9 differed from those observed in domestic animals. The cauda showed a pattern similar to that previously described. These results indicate that AQPs 1 and 9 have reversed locations and roles in rams, suggesting activity variations related with fluid and solute absorption throughout the epididymis.     

Unusual osteochondral lesions of the talus in a horse

A 2-year-old Thoroughbred gelding was evaluated for a grade 3 out of 5 unilateral hind limb lameness. Flexion of the right hock and stifle joints (spavin test) exacerbated the lameness. Response to intra-articular and perineural anaesthesia isolated the source of lameness to the tarsocrural area, despite an absence of tarsocrural joint effusion. Routine radiographic examination of the hock did not reveal any significant abnormalities. Skeletal nuclear scintigraphic evaluation revealed a focal region of increased bone activity in the proximal medial trochlear ridge of the talus. Flexed lateromedial radiographic views identified three discrete semicircular lytic lesions at the proximal articular margin of the medial trochlear ridge of the talus. Conservative management of the lesions was associated with a successful return to racing. The location and appearance of the osteochondral lesions of this report have not been previously reported and may be a manifestation of developmental orthopaedic disease and abnormal endochondral ossification. Nuclear scintigraphy and flexed lateromedial radiographic views facilitated identification of the lesions. This radiographic view is recommended when lameness is isolated to the tarsocrural joint and standard radio-graphic projections fail to identify a cause.