Aspects of the life cycle and pathogenesis of Elaphostrongylus alces in moose (Alces alces).

Aspects of the migratory life cycle and pathogenesis of Elaphostrongylus alces were studied in 7 randomly selected moose calves and 7 yearlings killed during August to November. One calf and 1 yearling were uninfected. The 6 infected calves had recent infections, whereas the 6 yearlings showed older infections from the summer of the previous year. The 2 calves killed in September had a total of 26 adult E. alces in the epidural space of the caudal vertebral canal and none in the skeletal muscles, whereas the remaining calves killed 1 to 2 mo later had 25 nematodes in the caudal and cranial vertebral canal and 7 in the skeletal muscles. The yearlings had a total of 101 adult E. alces in the skeletal muscles and 2 in the vertebral canal. There were no findings indicating involvement of the central nervous system in the life cycle of E. alces. Our findings suggest that E. alces migrates directly from the gut to the epidural space of the caudal vertebral canal where development to the adult stage takes place. During development, the nematode produces inflammation of the epidural tissue and spinal nerves. Development in the caudal vertebral canal is followed by some anterior dispersion of nematodes along the canal, and migration into skeletal muscles. Here the nematodes seem to live in reproductive pairs and groups. The predilection site for E. alces in moose is the muscles of the thigh.     

Attempts to Transfer Elaphostrongylus alces from Moose (Alces alces) to Sheep and Goats

Six 1 year old female and 6 four months old male goats were inoculated different numbers of E. alces third-stage larvae. Protostrongylid larvae were not detected in the faeces of these animals during the experiment. At the end of the experimental period the animals were euthanized and autopsied. Neither parasites nor pathological lesions related to larval or adult stages of E. alces could be demonstrated.     

The role of the urals in the genetic diversity of the European moose subspecies (Alces alces alces)

The genetic diversity of the Uralian moose population and the role of the Ural region in the phylogeographic structure of the European moose were evaluated based on sequence polymorphisms of the mtDNA control region. The nucleotide diversity of the Ural moose was low, whereas haplotype diversity was rather high. It was found that the haplotype pool of the Ural moose reflects both the unique features of their mitochondrial lineages and their connection with Alces alces alces populations of Europe and West Siberia. The structure of median networks and the territorial haplotype distribution support the hypothesis that the mitochondrial lineages typical for this part of the European moose area originate from a late Pleistocene refugium that was located in the Urals.     

Elaeophora schneideri in moose (Alces alces) from Colorado.

Two adult moose (Alces alces) from Colorado (USA) were naturally infected with Elaeophora schneideri. Both animals had patent infections indicating that moose may serve as definitive hosts. Gross and histological lesions were characterized by fibromuscular intimal proliferation within the carotid arteries and rete mirabile cerebri. This is the first report of Elaeophora schneideri in moose from Colorado.     

Carnivora: the primary structure of the giant otter (Pteronura brasiliensis, Mustelidae) hemoglobin

The hemoglobin of the Giant Otter (Pteronura brasiliensis, Carnivora) contains only one component. The complete primary structures of the alpha- and beta-chains are presented. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid- and gas-phase Edman degradation of the chains and their tryptic peptides. The alpha-chains show 18 and the beta-chains 12 exchanges compared with human alpha- and beta-chains, respectively. In the alpha-chains, two substitutions involve alpha 1/beta 1-contacts and one a heme-contact. In the beta-chains one alpha 1/beta 1-, one alpha 1/beta 2- and one heme-contact are exchanged. The alpha- and beta-chains of the Giant Otter are compared to those of the Common Otter and other Carnivora hemoglobins.     

Carnivora: the primary structure of the common otter (Lutra lutra, Mustelidae) hemoglobin

The hemoglobin of the Common Otter (Lutra lutra, Carnivora) contains only one component. The complete primary structures of the alpha- and beta-chains are presented. They were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas-phase Edman degradation of the chains and their tryptic peptides. The alpha-chains show 18 and the beta-chains 13 substitutions compared to human alpha- and beta-chains, respectively. In the alpha-chains one heme- and two alpha 1/beta 1-contacts are exchanged. In the beta-chains the replacements involve one heme-, one alpha 1/beta 1-, and one alpha 1/beta 2-contact. The alpha- and beta-chains of the Common Otter are compared to those of other Carnivora hemoglobins. The unexpected low number of substitutions between Common Otter hemoglobin and that of Lesser Panda as well as of Harbor Seal is discussed.     

The primary structure of the hemoglobin of the greylag goose (Answer anser) and the unequal evolution of the beta-chains (an experimental approach to a biochemical analysis of behaviour (author's transl)]

The primary structures of the alpha- and beta-chains from greylag goose (Anser anser) hemoglobin are given. The sequence was deduced automatically in the sequenator. They differ from chicken alpha-chains in the exchange of 30, from beta-chains in the exchange of only 8 amino acid residues, respectively. The contact points of inositol pentaphosphate with the beta-chains are identical in chicken and greylag goose. Unequal evolution of the beta-chains was found, which is published here for the first time. By comparing the sequences of chicken and greylag goose and considering paleontological data, we found the mutation rate of the alpha-chains to be normal, i.e. 6 million years/mutation. This corresponds to the values for other species. The mutation rate of beta-chains is reduced and was calculated at 25 million years/mutation. This is possibly due to a specific function of beta-chains. This paper is the basis of our attempt to explain on a molecular basis the ability of bar-headed goose (Anser indicus) to fly and breathe at high altitudes.     

The primary structure and functional properties of the hemoglobins of a ground squirrel (Spermophilus townsendii, Rodentia)

The hemoglobin of the ground squirrel Spermophilus townsendii consists of two components which are present in a ratio of ca. 2:1. The two hemoglobins have identical alpha-chains, but differ in their beta-chains. We present the primary structures of the alpha- and the two beta-globin chains. Following chain separation by chromatography on carboxymethyl-cellulose CM-52, the amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides, as well as of a peptide obtained by acid hydrolysis of the Asp-Pro bond of the beta-chains. The two beta-chains differ by only one amino-acid residue, Ala being present in the main and Asp in the minor component in position 58 (E2). The comparison with human hemoglobin showed only 14 exchanges in the alpha-chains but 33 in the beta-chains. Whereas no contact positions are affected in the alpha-chains, we found four such substitutions in the beta-chains, including one heme contact, two alpha 1/beta 1-contacts, and one alpha 1/beta 2-contact. It seems however, that the substitution found in the beta-chains has no effect on the oxygen affinity.     

Intrinsic oxygen affinity of hemoglobins: the hemoglobin of bisons (Bison bonasus,Bovidae)

The hemoglobin from a European Bison (Bison bonasus) was analysed and the complete primary structures of the alpha I-, alpha II-and beta-chains have been determined. The alpha I- and alpha II-chains differ only at position alpha 19 (Asp----Gly). The beta-chains are homogeneous. The sequences are compared with the globin chains of Bison bison and bovine and the polymorphism of the alpha-chains is discussed. On the basis of the primary structure it may be concluded that the hemoglobin of Bison bonasus belongs to the group of hemoglobins with intrinsically low oxygen affinity.     

The primary structure of the hemoglobin of the electric eel (Electrophorus electricus)

The blood of the Electric Eel contains only one hemoglobin component. The primary structures of the alpha- and beta-chains are presented. These were separated by high-performance liquid chromatography, using a new kind of buffer system. The alpha-chains are acetylated, and consist of 142 residues, while the beta-chains are not blocked, and consist of 147 residues. The phylogenetic distances between these and the alpha- and beta-chains of human hemoglobin are 48 and 50% amino-acid exchanges, respectively. The relationship between primary structure and the Bohr effect and Root effect is discussed, especially the significance of the serine found in position F9 beta.     

Parasites of moose (Alces alces) from an agricultural area of eastern Ontario

Viscera of 16 moose and hide samples of 24 moose (Alces alces) shot in eastern Ontario in 1985 were examined for parasites. Two species of trematodes, one species of cestode, five species of nematodes and one species of tick were recovered. One nematode species, Trichuris discolor, is reported for the first time from moose. Our results suggest that the parasite fauna of the moose may have been influenced by the absence or scarcity of other species of wild cervids or carnivores and by the presence of domestic livestock.     

Carnivora: the primary structure of the Pacific Walrus (Odobenus rosmarus divergens, Pinnipedia) hemoglobin

The primary structure of the alpha- and beta-chains of the hemoglobin from the Pacific Walrus (Odobenus rosmarus divergens, Pinnipedia) is presented. Sequence analysis revealed only one hemoglobin component whereas two bands were found in polyacrylamide gel electrophoresis. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid- and gas-phase sequencing of the chains and their tryptic peptides. The alpha-chains show 20 and the beta-chains 12 exchanges compared to the corresponding human chains. In the alpha-chains one heme- and two alpha 1/beta 1-contacts were exchanged whereas in the beta-chains one alpha 1/beta 1-, one alpha 1/beta 2-and one heme-contact are substituted. Compared to Harbour Seal (Phoca vitulina) the Walrus hemoglobin shows 9 amino-acid replacements in the alpha-chains and 5 in the beta-chains. The relation between Pinnipedia and Arctoidea is discussed.     

Dermacentor albipictus on moose (Alces alces) in Ontario.

Fifty-five moose (Alces alces) collected from 1963 to 1965 in the Chapleau Crown Game Preserve of northern Ontario were examined for ectoparasites. Dermacentor albipictus was the only parasite recovered. D. albipictus was absent from 15 moose examined during June, July and August; first observed on 1 or 2 moose examined in September; and present on all 38 moose collected from October to May. Ticks were not evenly distributed on the body. Infestations varied from 32 to 13,490 ticks/moose for 14 individuals. Levels of infestation observed did not have an obvious adverse effect on the health of the moose.     

Mitochondrial phylogeography of moose (Alces alces): late pleistocene divergence and population expansion

We examined phylogeographic relationships of moose (Alces alces) worldwide to test the proposed existence of two geographic races and to infer the timing and extent of demographic processes underpinning the expansion of this species across the Northern Hemisphere in the late Pleistocene. Sequence variation within the left hypervariable domain of the control region occurred at low or moderate levels worldwide and was structured geographically. Partitioning of genetic variance among regions indicated that isolation by distance was the primary agent for differentiation of moose populations but does not support the existence of distinct eastern and western races. Levels of genetic variation and structure of phylogenetic trees identify Asia as the origin of all extant mitochondrial lineages. A recent coalescence is indicated, with the most recent common ancestor dating to the last ice age. Moose have undergone two episodes of population expansion, likely corresponding to the final interstade of the most recent ice age and the onset of the current interglacial. Timing of expansion for the population in the Yakutia--Manchuria region of eastern Asia indicates that it is one of the oldest populations of moose and may represent the source of founders of extant populations in North America, which were colonized within the last 15,000 years. Our data suggest an extended period of low population size or a severe bottleneck prior to the divergence and expansion of extant lineages and a recent, less-severe bottleneck among European lineages. Climate change during the last ice age, acting through contraction and expansion of moose habitat and the flooding of the Bering land bridge, undoubtedly was a key factor influencing the divergence and expansion of moose populations.     

The primary structure of the hemoglobin of the Indian false vampire (Megaderma lyra, Microchiroptera)

The hemoglobin of the Indian false vampire Megaderma lyra contains only one component. In this paper, we are presenting its primary structure. The globin chains were separated by high-performance liquid chromatography and the sequences determined by automatic liquid and gas phase Edman degradation of the chains and their tryptic peptides, as well as of the prolyl-peptides obtained by acid hydrolysis of the Asp-Pro bond in the alpha- and beta-chains. The alpha-chains show 23 and the beta-chains 20 exchanges compared with the human alpha- and beta-chains, respectively. In the alpha-chains, three exchanges involved alpha 1/beta 1 contacts. In the beta-chains one heme-and three alpha 1/beta 1 contacts are exchanged. The functional and systematic aspects of these replacements are discussed.     

Growth and development of winter tick, Dermacentor albipictus, on moose, Alces alces

Moose, Alces alces, were infested with 21,000 or 42,000 larval Dermacentor albipictus at the end of September. Larvae grew rapidly and molted to the nymphal stage 10-22 days after infestation. The nymphal stage lasted approximately 3 mo until mid-January and was characterized by a diapause. The diapause is likely an adaptation to survival in cold climates. Nymphs started engorging in January and adults were seen with increasing abundance from mid-January to March and April. The minimum parasitic period was 175 days. Growth of larvae and nymphs was similar on moose given different numbers of larvae and was generally similar between a moose infested in November and moose infested earlier. Dimensions and stages of development throughout the parasitic phase are given. Game enforcement officers are encouraged to use these data for determination of season of death of moose.     

Carnivora: primary structure of the hemoglobins from ratel (Mellivora capensis)

The erythrocytes of adult ratel contain two hemoglobin components, with two alpha- and one beta-chains. In this paper, their complete amino acid sequences are presented. The two alpha-chains differ in one residue at position 34 (Ala----Val) only. The primary structure of the chains was determined by sequencing the N-terminal regions (45 steps) and the tryptic peptides after their isolation from the digests by reversed-phase high-performance liquid chromatography. The alignment of these peptides was deduced from homology with other carnivora globins. The alpha-chains show 21 and the beta-chains 11 exchanges compared with human globin chains. In the alpha-chains, one heme- and two alpha 1/beta 1 contacts are exchanged. In the beta-chains there are three exchanges which involve one alpha 1/beta 1-, one alpha 1/beta 2- and one heme-contact. Between the ratel hemoglobin and those of carnivora a high degree of homology was found.     

Carnivora: primary structure of the hemoglobin from the spotted hyena (Crocuta crocuta, Hyenidae)

The primary structure of the alpha- and beta-chains of hemoglobin from spotted hyena (Crocuta crocuta, Hyenidae) is presented. The structure-function relationship is discussed. The separation of the chains directly from hemoglobin was performed by RP-HPLC. After tryptic digestion of the chains, the peptides were isolated by RP-HPLC. Amino-acid sequences were determined by Edman degradation in liquid- and gas-phase sequencers. The alignment of the tryptic peptides was made by homology with human and other Carnivora hemoglobins. The hemoglobin from spotted hyena (Crocuta crocuta) exhibits in its alpha- and beta-chains 22 and 20 exchanges, respectively, compared to human hemoglobin. In the alpha-chains, two alpha 1 beta 1-contacts are exchanged. In the beta-chains five exchanges involve one alpha 1 beta 1-contact, one alpha 1 beta 2-contact, one heme contact, and two 2,3-DPG-binding sites.     

Carnivora: the primary structure of the beach marten (Martes foina, Mustelidae) hemoglobin

The primary structures of alpha- and beta-chains from the hemoglobin of the Beach Marten (Martes foina, Carnivora) are presented. The globin chains were separated on CM-cellulose in 8M urea buffer. The amino-acid sequences were established by automatic liquid- and gas-phase Edman degradation of the intact chains and the tryptic peptides from oxidized chains. Comparison of the sequences with human hemoglobin shows 21 exchanges in the alpha- and 12 in the beta-chains. The differences concerning heme and interchain contact sites as well as the substitution alpha 77 (EF6)Pro----Ala are discussed. The latter is observed for the first time in a mammalian hemoglobin. The sequences are compared with those of other Carnivora. The beta-chains of Martes foina and Pteronura brasiliensis (Giant Otter) are found to be identical, but their alpha-chains differ in 7 positions. The surprising small numbers of exchanges between the hemoglobin from Beach marten and that from Lesser and Greater Panda are discussed.