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Interaction in replication between goose parvovirus strain B and duck plague herpesvirus.

The goose parvovirus strain B was found to replicate only in cells with DNA synthesis. Cells in the stationary phase of DNA synthesis or maintained under 2 mM thymidine (TdR) in excess were refractive to the parvovirus infection. However, stationary phase cells could be rendered to produce progeny paroviruses by herpesvirus superinfection. In reverse, the replication of the herpesvirus was significantly inhibited by parvovirus preinfection of cells.

Animals↗

Bluetongue virus hemagglutination and its inhibition by specific sera.

Bluetongue-virus (BTV) was found to agglutinate a variety of erythrocytes including sheep-, chicken-, guinea pig- and mouse-erythrocytes. Hemagglutination was inhibited specifically with type specific serum. A temperature dependence was only found for chicken erythrocytes, which showed a hemagglutination optimum at 37 degrees C. The hemagglutination was lost upon treatment of the virus with 0.4% trypsin as well as after treatment with 0.01 M KJO4. Heating of the virus preparation to 56 degrees C resulted in the loss of the HA-activity. Gelchromatographic studies indicated that the hemagglutinating capacity is associated with the complete virion. Whereas virulent strains of BTV hemagglutinate a number of different erythrocytes the avirulent type tested produced only a slight hemagglutination with sheep red blood cells. However, specific antiserum produced with the avirulent strain yielded strong hemagglutination inhibition (HI) with the corresponding virulent strain. Treatment of sera prior to their use in the HI proved necessary to remove nonspecific inhibitors. The efficiency of KJO4 in removing nonspecific inhibitors. The efficiency of KJO4 in removing nonspecific inhibitors indicates that carbohydrates represent the major group of nonspecific inhibitors. The data represented recommended the hemagglutination inhibition tests as a new method to identify the various BTV serotypes.

Animals↗

Radial haemolysis in gel: a comparative study with Chikungunya, Japanese encephalitis and rubella viruses, representatives of three genera of Togaviridae family.

Optimal conditions of radial haemolysis in gel (HIG) with Chikungunya (Chik) and Japanese encephalitis (JE) viruses were developed and compared with those of rubella virus. Sheep erythrocytes were found preferable for HIG with Chik and JE viruses, unlike rubella virus, where goose erythrocytes gave best results. Rooster erythrocytes were completely negative in the Chik and JE HIG, again differing from rubella virus, which was practically as good with rooster as with goose erythrocytes. Sheep erythrocytes with rubella virus gave incomplete reactions in HIG. Sensitization of erythrocytes with JE and Chik viruses is better, when borate-phosphate, and not phosphate buffer, is used. Optimum pH values for both viruses should be regarded. Sucrose-acetone, freon and borate-saline antigens from infected mice brain may be used for HIG with Chik and JE viruses.

Animals↗

Perpetuation of influenza A viruses in Alaskan waterfowl reservoirs.

To provide information on the mechanism of perpetuation of influenza viruses among waterfowl reservoirs in nature, virological surveillance was carried out in Alaska during their breeding season in summer from 1991 to 1994. Influenza viruses were isolated mainly from fecal samples of dabbling ducks in their nesting places in central Alaska. The numbers of subtypes of 108 influenza virus isolates were 1 H2N3, 37 H3N8, 55 H4N6, 1 H7N3, 1 H8N2, 1 H10N2, 11 H10N7, and H10N9. Influenza viruses were also isolated from water samples of the lakes where they nest. Even in September of 1994 when the most ducks had left for migration to south, viruses were still isolated from the lake water. Phylogenetic analysis of the NP genes of the representative isolates showed that they belong to the North American lineage of avian influenza viruses, suggesting that the majority of the waterfowls breeding in central Alaska migrate to North America and not to Asia. The present results support the notion that influenza viruses have been maintained in waterfowl population by water-borne transmission and revealed the mechanism of year-by-year perpetuation of the viruses in the lakes where they breed.

Alaska↗

Electrolyte transport by gallbladders of rabbit and guinea pig: effect of amphotericin B and evidence of rheogenic Na transport.

Ion transport and electrical properties of rabbit and guinea pig gallbladders were investigated to gain further information about the active transport mechanism that mediates fluid absorption. The intracellular and transepithelial electrical potentials were measured simultaneously using the microelectrode technique. Exposure of the mucosal surface to Amphotericin B resulted in the prompt development of a serosa-positive electrical potential difference (PD) which could not be attributed to an alteration in ion diffusion potentials across either the cell membrane or across the tight junction. Because the Amphotericin B-induced PD was immediately dependent on warm temperatures and O2, and was independent of NA and K concentration gradients across the cell membrane, it is suggested that active ion transport is directly responsible for the PD. Since the PD was abolished in the absence of Na in the bathing solutions, a rheogenic Na pump is postulated; this pump also appears to be operative in tissues not exposed to Amphotericin B. The specific tissue properties altered by Amphotericin B to produce a serosa-positive PD remain incompletely defined. The results of the present study indicate that ion transport by rabbit gallbladder in vitro is a consequence of a rheogenic active Na transport mechanism at the basolateral membranes which, in conjunction with a coupled NaC1 influx process at the mucosal border, ultimately results in absorption of NaC1 and water.

Amphotericin B↗

Electrical parameters in gallbladders of different species. Their contribution to the origin of the transmural potential difference.

Amphotericin B enhances Na+ conductance of the mucosal membrane of gallbladder epithelial cells and in such a way it modifies the brush border electromotive force. On this basis a method to measure cell and shunt resistances by comparing changes of the mucosal membrane potential (Vm) and of the transmural p.d. (Vms) is developed. This method is applied in gallbladders of different vertebrate species (i.e. rabbit, guinea pig, goose, tortoise, toad, trout). The two tested mammals, rabbit and guinea pig, exhibited a lower shunting percentage (89--93%) than the nonmammals (96--97%), but this fact did not bring about a homogeneous positive Vms. This means that shunting percent contributes, but it is not the only source of differences in Vms, in accordance with that reported by Gelarden and Rose (J. Membrane Biol. 19:37, 1974). Moreover, mammals exhibited a lower luminal resistance and a lower ratio between luminal and basolateral resistance than nonmammals. Possible causes of these differences are discussed.

Amphotericin B↗

Common antigenic properties of a g-type (goose) and a c-type (duck) egg white lysozyme: antibody responses in rabbits and mice.

Embden goose (GEWL) and Barbary duck (DEWL) egg white lysozymes possess different amino acid sequences corresponding to the g-type and c-type, respectively. GEWL was shown to be a better immunogen than DEWL in both rabbits and mice. The antigenicity of the two lysozymes was tested using different techniques (i.e. indirect ELISA, inhibition tests and immunoabsorption experiments). Injection of either GEWL or DEWL into rabbits and mice induced both specific antibodies and cross-reacting antibodies. Moreover, anti-GEWL antibodies, in contrast to anti-DEWL antibodies, did not cross-react with hen egg white lysozyme (HEWL), a c-type lysozyme. While the structure of GEWL was not modified after binding to plastic, DEWL was denaturated, but it did keep some native epitopes. It was concluded that g-type and c-type lysozymes, which have different amino acid sequences, exhibit strong common antigenic properties.

Animals↗

Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution.

The three-dimensional structure of goose-type lysozyme (GEWL), determined by x-ray crystallography and refined at high resolution, has similarities to the structures of hen (chicken) egg-white lysozyme (HEWL) and bacteriophage T4 lysozyme (T4L). The nature of the structural correspondence suggests that all three classes of lysozyme diverged from a common evolutionary precursor, even though their amino acid sequences appear to be unrelated (Grütter et al. 1983). In this paper we make detailed comparisons of goose-type, chicken-type, and phage-type lysozymes. The lysozymes have undergone conformational changes at both the global and the local level. As in the globins, there are corresponding alpha-helices that have rigid-body displacements relative to each other, but in some cases corresponding helices have increased or decreased in length, and in other cases there are helices in one structure that have no counterpart in another. Independent of the overall structural correspondence among the three lysozyme backbones is another, distinct correspondence between a set of three consecutive alpha-helices in GEWL and three consecutive alpha-helices in T4L. This structural correspondence could be due, in part, to a common energetically favorable contact between the first and the third helices. There are similarities in the active sites of the three lysozymes, but also one striking difference. Glu 73 (GEWL) spatially corresponds to Glu 35 (HEWL) and to Glu 11 (T4L). On the other hand, there are two aspartates in the GEWL active site, Asp 86 and Asp 97, neither of which corresponds exactly to Asp 52 (HEWL) or Asp 20 (T4L). (The discrepancy in the location of the carboxyl groups is about 10 A for Asp 86 and 4 A for Asp 97.) This lack of structural correspondence may reflect some differences in the mechanisms of action of the three lysozymes. When the amino acid sequences of the three lysozyme types are aligned according to their structural correspondence, there is still no apparent relationship between the sequences except for possible weak matching in the vicinity of the active sites.

Amino Acid Sequence↗

Random walking.

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Altitude↗