Lead poisoning in captive Andean condors (Vultur gryphus)

Elevated lead in the tissues of raptors, especially those that scavenge, is a common occurrence, and lead poisoning appears to be a significant problem in the ongoing recovery effort for California condors (Gymnogyps californianus). Elevated blood lead levels have been found in released birds, and a number of birds have died of lead poisoning. In earlier work, we dosed turkey vultures (Cathartes aura) with lead shot but found them to be a poor model for lead poisoning. In this study, we dosed four Andean condors (Vultur gryphus) with lead shot and found them to be quite sensitive, as two of the birds died and the other two exhibit signs of lead poisoning within 50 days. All lead-responsive parameters were affected, and regurgitation of dosed shot occurred only once. The response of the Andean condors appeared to mimic California condors, suggesting that once exposed to lead, the possibility of survival is poor. This is consistent with observations in the wild, where otherwise healthy birds exposed to metallic lead quickly succumb. At the very least, the release program has to maintain constant surveillance and an active lead monitoring program.     

The hemoglobins of the adult blackbird (Turdus merula, Passeriformes). The sequence of the major (HbA) and minor component (HbD)

The blood of the adult blackbird contains one major hemoglobin component (HbA = alpha A2, beta 2, ca. 80%) and one minor one (HbD = alpha D2 beta 2, ca. 20%). The Hb-components were separated by FPLC on a TSK SP-5 PW column, and eluted with a linear NaCl gradient, while the globin chains were purified on a cation exchange (CM-Cellulose). Tryptic peptides from the globin chains were separated by HPLC on an RP-2 Lichrosorb column. The complete amino acid sequence was determined by automatic Edman degradation, using film and gas phase methods. For the alpha A-, alpha D- and beta-chains, peptide alignment was carried out relative to the corresponding chains of the greylag goose (Anser anser). The close phylogenetic relationship between blackbird, tree sparrow and starling is verified by the hemoglobin sequence. The O2-affinities of the major and minor hemoglobin components of the blackbird are not yet known. Thus, the results were interpreted on the basis of primary structure. Substitutions of possible structural significance were examined with the help of molecular graphics/modelling.     

Protein electrophoresis in Andean condors (Vultur gryphus): Reference values and differences between wild and rehabilitating individuals

The study of wildlife health greatly contributes to understanding population dynamics and detecting conservation threats. The determination of the different fractions of plasma proteins (proteinogram) is an important laboratory tool to study wildlife health. The aim of this study was to characterize protein electrophoresis in wild Andean condors (Vultur gryphus) from north‐western Patagonia and to evaluate differences according to age and sex classes. Once reference values of wild, apparently healthy individuals, were established, we compared these values to those of individuals received at the Buenos Aires Zoo in Argentina for rehabilitation due to various health problems. Reference proteinograms from wild Andean condors differed only in the α 1 and β 2‐fractions between sex categories. Males showed higher concentrations of these protein fractions than females. We found clear differences between wild birds and rehabilitating individuals. Total proteins, globulins, α 1‐globulins, total α‐globulins, β 2‐globulins, total β‐globulins, and γ‐globulins were significantly higher in rehabilitating than in wild individuals, whereas albumin, α 2, and β1‐globulins were similar between these groups. The albumin/globulin ratio, as a general indicator of health, was significantly lower in rehabilitating than in wild individuals. The results indicate the effects on different protein fractions of pathologic processes occurring in individuals undergoing rehabilitation. Our results provide useful insights, contributing to improving diagnoses and prognoses in this species. This information may also be useful to assess the health status of Andean condors in studies of wild populations and for comparisons with other bird species.     

Genomic data reveal international lineages of critical priority Escherichia coli harbouring wide resistome in Andean condors (Vultur gryphus Linnaeus, 1758)

Critical priority pathogens have globally disseminated beyond clinical settings, thereby threatening wildlife. Andean Condors (Vultur gryphus) are essential for ecosystem health and functioning, but their populations are globally near threatened and declining due to anthropogenic activities. During a microbiological and genomic surveillance study of critical priority antibiotic‐resistant pathogens, we identified pandemic lineages of multidrug‐resistant extended‐spectrum β‐lactamase (ESBL)‐producing Escherichia coli colonizing Andean Condors admitted at two wildlife rehabilitation centres in South America. Genomic analysis revealed the presence of genes encoding resistance to hospital and healthcare agents among international E. coli clones belonging to sequence types (STs) ST162, ST602, ST1196 and ST1485. In this regard, the resistome included genes conferring resistance to clinically important cephalosporins (i.e., CTX‐M‐14, CTX‐M‐55 and CTX‐M‐65 ESBL genes), heavy metals (arsenic, mercury, lead, cadmium, copper, silver), pesticides (glyphosate) and domestic/hospital disinfectants, suggesting a link with anthropogenic environmental pollution. On the other hand, the presence of virulence factors, including the astA gene associated with outbreak of childhood diarrhoea and extra‐intestinal disease in animals, was identified, whereas virulent behaviour was confirmed using the Galleria mellonella infection model. E. coli ST162, ST602, ST1196 and ST1485 have been previously identified in humans and food‐producing animals worldwide, indicating that a wide resistome could contribute to rapid adaptation and dissemination of these clones at the human–animal–environment interface. Therefore, these results highlight that Andean Condors have been colonized by critical priority pathogens, becoming potential environmental reservoirs and/or vectors for dissemination of virulent and antimicrobial‐resistant bacteria and/or their genes, in associated ecosystems and wildlife.     

Andean Condor (Vultur gryphus) in Ecuador: Geographic Distribution,Population Size and Extinction Risk

The Andean Condor (Vultur gryphus) in Ecuador is classified as Critically Endangered. Before 2015, standardized and systematic estimates of geographic distribution, population size and structure were not available for this species, hampering the assessment of its current status and hindering the design and implementation of effective conservation actions. In this study, we performed the first quantitative assessment of geographic distribution, population size and population viability of Andean Condor in Ecuador. We used a methodological approach that included an ecological niche model to study geographic distribution, a simultaneous survey of 70 roosting sites to estimate population size and a population viability analysis (PVA) for the next 100 years. Geographic distribution in the form of extent of occurrence was 49 725 km². During a two-day census, 93 Andean Condors were recorded and a population of 94 to 102 individuals was estimated. In this population, adult-to-immature ratio was 1:0.5. In the modeled PVA scenarios, the probability of extinction, mean time to extinction and minimum population size varied from zero to 100%, 63 years and 193 individuals, respectively. Habitat loss is the greatest threat to the conservation of Andean Condor populations in Ecuador. Population size reduction in scenarios that included habitat loss began within the first 15 years of this threat. Population reinforcement had no effects on the recovery of Andean Condor populations given the current status of the species in Ecuador. The population size estimate presented in this study is the lower than those reported previously in other countries where the species occur. The inferences derived from the population viability analysis have implications for Condor management in Ecuador. This study highlights the need to redirect efforts from captive breeding and population reinforcement to habitat conservation.     

The complete amino acid sequence of the major component myoglobin of Amazon river dolphin (Inia geoffrensis).

The complete amino acid sequence of the major component myoglobin from Amazon River dolphin, Inia geoffrensis, was determined by specific cleavage of the protein to obtain large peptides which are readily degraded by the automatic sequencer. Three easily separable peptides were obtained by cleaving the protein with cyanogen bromide at the methionine residues and four peptides were obtained by cleaving the methyl-acetimidated protein with trypsin at the arginine residues. From these peptides over 85% of the sequence was completed. The remainder of the sequence was obtained by fragmentation of the large cyanogen bromide peptide with trypsin. This protein differs from that of the common porpoise, Phocoena phocoena, at seven positions, from that of the common dolphin, Delphinus delphis, at 11 positions, and from that of the sperm whale, Physeter catodon, at 15 positions. By comparison of this sequence with the three-dimensional structure of sperm whale myoglobin it appears that those residues close to the heme group are most conserved followed by those in nonhelical regions and lastly by those in the helical segments. All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm whale myoglobin.     

High-altitude respiration of birds. The primary structures of the major and minor hemoglobin component of adult goshawk (Accipiter gentilis, Accipitrinae)

The primary structures of the hemoglobin components Hb A and Hb D of the adult Goshawk (Accipiter gentilis) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. Component separation was achieved by FPLC-chromatography on a TSK SP-5PW column in phosphate-buffers with a linear gradient of NaCl. The amino-acid sequences were established by automated Edman degradation of the globin chains and of the tryptic peptides in liquid-phase and gas-phase sequenators. The sequences are aligned with those of European Black Vulture (Aegypius monachus). Phylogenetic aspects and physiological properties for Goshawk hemoglobin are inferred from sequence data. A detailed evaluation of the oxygen-binding properties has been carried out during a prolonged study of the noteworthy ability of Falconiformes to cope with extremely low oxygen partial pressures, and will be the subject of a forthcoming paper.     

The amino acid sequence of the major parvalbumin of the whiting (Gadus merlangus).

1. The amino acid sequence of the major parvalbumin of the Whiting has been determined; the polypeptide chain is made of 108 residues, the terminal amino acid group is acetylated, there is no disulfide bridges, the structure of the two calcium binding sites is preserved and the distribution along the polypeptide chain of the hydrophobic residues implicated in the compact hydrophobic core of the protein is also maintained. 2. The comparison of this amino acid sequence with other parvalbumins indicates that it belongs to the beta type and that within the Gadidae family two types of parvalbumins also occur.     

Complete amino acid sequence of the major component myoglobin of finback whale (Balaenoptera physalus)

The complete amino acid sequence of the major component myoglobin from finback whale, Balaenoptera physalus, was determined by the automated Edman degradation of several large peptides obtained by specific cleavages of the protein. Three easily separable peptides were obtained by cleaving with cyanogen bromide at the two methionine residues and one large peptide was isolated after cleavage with (2-p-nitrophenylsulfenyl)-3-methyl-3'-bromoindolenine. More than 60% of the covalent structure was established by the sequential degradation of three of these peptides and the apomyoglobin. An additional 30% of the primary sequence was established with peptides obtained from tryptic digestion of both the apomyoglobin and the acetimidoapomyoglobin, and the final 10% of the sequence was completed after digestion of the two larger cyanogen bromide peptides with S. aureus strain V8 protease. This myoglobin differs from that of the sperm whale, Physeter catodon, at 15 positions, from that of the arctic minke whale, Balaenoptera acutorostrata, at 3 positions, and from that of the California gray whale, Eschrichtius gibbosus, at 4 positions. All of the substitutions observed in this sequence fit easily into the three-dimensional structure of the sperm whale myoglobin.     

Hemoglobins of reptiles. The primary structure of the major and minor hemoglobin component of adult Western Painted Turtle (Chrysemys picta bellii)

Red blood cells of adult Western Painted Turtles (Chrysemys picta bellii) contain two hemoglobin components: HbA (alpha A2 beta 2) and HbD (alpha D2 beta 2). We present the complete amino-acid sequences of the alpha A-chains from the major component and of the beta-chains common to both components. Structural features are discussed with respect to the animals extreme tolerance of severe hypoxic conditions during hibernation which is accompanied by a high oxygen affinity of the hemoglobin. The strong ATP dependence of Western Painted Turtle hemoglobin oxygen affinity is contrasted by the loss of one ATP-binding site, beta 143(H21)-Arg----Leu. The primary structure of the beta-chains excludes an allosteric control mechanism by hydrogencarbonate as it was found in crocodiles. Except in turtles a hemoglobin pattern with HbA and HbD sharing the same beta-subunits has been found only in birds. In comparison to other vertebrate hemoglobins there is a surprising similarity of the sequences to those of bird hemoglobins. alpha A- as well as alpha D-chains show larger homologies to chains of the same type in different species than alpha A- and alpha D-chains to each other in the same species. This indicates a duplication of the alpha-gene preceding the divergence of turtles and birds.     

High altitude respiration of birds. The primary structures of the major and minor hemoglobin component of adult European black vulture (Aegypius monachus, Aegypiinae)

The primary structures of the hemoglobin components Hb A and Hb D of the European Black Vulture (Aegypius monachus) are presented. The globin chains were separated on CM-Cellulose in 8M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the globin chains and the tryptic peptides in liquid phase and gas-phase sequenators. The sequences are compared with those of the Golden Eagle, and with those of the Andean Condor, a New World vulture. The possible evolutionary significance of the alpha D-chains is considered. This paper serves as a reference study for high-altitude respiration of Falconiformes.     

Carnivora: the primary structure of the major hemoglobin component from adult European lynx (Lynx lynx, Felidae).

The complete primary structure of the major hemoglobin component from the adult European lynx (Lynx lynx) is presented. Presence of two hemoglobin components and three chains, A, B, and , identified by gel electrophoresis. The purification of the globin chains achieved by ion-exchange chromatography. The globin chains were digested with trypsin. The peptide generated were purified by reversed-phase HPLC. Sequencing of the native chains up to 42 cycles and of the tryptic peptides were deduced by Edman degradation in liquid- and gasphase sequencer. The primary structure established aligned with those of human Hb-A. The comparison of lynx globin chains with other representatives of the Felidae, lion, tiger, jaguar, leopard, and cat revealed high homology.Deceased on May 27, 1989.