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We report an outbreak of botulism that occurred in July 2002 in a group of 12 Alaskan Yu'pik Eskimos who ate blubber and skin from a beached beluga whale. Botulism death rates among Alaska Natives have declined in the last 20 years, yet incidence has increased.
Bronchopneumonia was observed at the necropsy of a North Atlantic pilot whale (Globicephala melaena). The areas of necrosis were well circumscribed clusters, disseminated throughout the left lung. Streptococcus equi was isolated in pure culture from the lung parenchyma, pharynx and pericardial fluid.
Approximately 3.5 mo following its capture, a beluga whale (Delphinapterus leucas) developed focal pale gray skin lesions. These lesions persisted for at least 8 mo. A biopsy from one of these sites revealed epithelial intranuclear inclusions. Herpes-like viral particles were seen by transmission electron microscopy. The eventual regression of skin lesions and lack of other clinical signs suggests the virus was only mildly pathogenic in this animal.
A fractured right mandible with midlength nonunion and oral lesions were noted in a subsistence-harvested female bowhead whale (Balaena mysticetus) near Wainwright, Alaska (USA). The cause of the fracture was not apparent. The fracture resulted in misalignment of the mandible. The abnormal mobility at the fracture site probably caused irregular baleen stowage within the oral cavity, leading to breakage of many baleen plates and extensive ulceration of the tongue and lips. Good body condition suggested the fracture was not debilitating.
A study of the microbiological flora isolated from cultures of normal and lesional skin tissue samples collected from 19 bowhead whales (Balaena mysticetus) over a 4 yr period is presented. These cultures were obtained from 30 tissue samples (17 normal, 13 lesion) and 248 swab samples (157 normal, 91 lesion). Seven hundred-thirty bacterial and yeast isolations were made (285 normal, 445 lesion). Distribution revealed that 56% of the gram positive bacterial isolates, 75% of the gram negative bacterial isolates and 64% of the yeast isolates recovered were associated with lesional skin. It was found that 80% of one group of Corynebacterium sp. isolates, 90% of the Acinetobacter sp. isolates and 94% of the Moraxella sp. isolates were associated with lesional skin. Although the primary yeasts recovered were Candida spp., they were found on both normal and lesional skin. Enzymatic assays of isolates from normal and lesional skin demonstrated production of enzymes capable of causing necrosis. The majority of the microorganisms recovered were facultative anaerobes and many of them could be considered potential pathogens of mammalian hosts.
Mammary secretions from two bowhead whale (Balaena mysticetus L.) females carrying near-term fetuses were analyzed for dry matter, ash, protein, fat, carbohydrate and energy content. Protein values ranged from 75.9% to 97.3% of dry matter. Fat ranged from 0.6% to 9.1% of dry matter. A protein corresponding to beta-lactoglobulin on gel filtration chromatography was the predominant whey protein. Neutralizing antibodies to nine caliciviruses were detected in one sample. Composition of these two samples differs from previous reports for cetacean milk, perhaps due to the stage of lactation.
An adult female bowhead whale, Balaena mysticetus, from the Beaufort Sea, Alaska (USA), had necrosis of a well-demarcated portion of the mid-jejunum and adjacent mesentery, accompanied by fibrinous peritonitis. The veins within the mesentery adjacent to the affected intestine were severely dilated and hyperemic. There were no perforations of the gastrointestinal tract, nor any thromboses within the mesenteric veins. Death appeared due to the sequelae of intestinal volvulus and infarction; reduction of the displacement presumably occurred during handling of the animal.
A hermaphrodite beluga whale (Delphinapterus leucas) was found in the St. Lawrence Estuary, Québec, Canada. This animal had two testicles, two separate ovaries, and the complete ducts of each sex; cervix, vagina and vulva were absent. Mature spermatozoa were found in the lumen of seminiferous tubules in the testicles, and numerous involuted corpora lutea were recognized in the ovaries. This represents the first case of true hermaphroditism in a cetacean, and is the fourth hermaphrodite mammal with two testicles and two separate ovaries.
A case of uterine adenocarcinoma is reported in a 26-yr-old, free-ranging beluga whale (Delphinapterus leucas) from the St. Lawrence estuary (Quebec, Canada). This neoplasm appeared as a segmental stenotic thickening of the left uterine horn composed of well differentiated, but disorganized and infiltrative, glandular structures surrounded by an extensive scirrhous stroma. Abdominal carcinomatosis was observed on the mesosalpinx and on the serosal aspect of the gastric compartments. This is the first report of a malignancy originating in the uterus of a cetacean.
Specific catalytic oxidation of sperm whale oxymyoglobin by small amounts of potassium ferri- and ferrocyanide, from 1 to 20% in relation to the protein concentration, was studied. The mechanism of catalysis was shown to involve specific binding of the ferrocyanide anion to the protein. The influence of pH and ionic strength of the medium, the [Fe(CN)6]4- concentration and of chemical modification of Mb histidines by bromoacetate, as well as the effect of the Mb complexing with redox-inactive zinc ion on the rate of reaction was examined. The zinc ion forms a stable complex with His 119(GH1) on the Mb surface at the equimolar Zn2+ concentration. The kinetic scheme of the reaction was analyzed, and the equilibrium and kinetic parameters were obtained. It was first shown that the strong oxidant such as potassium ferricyanide is able to react with the same protein by two distinct mechanisms: (i) a simple outer sphere electron transfer over the heme edge and (ii) electron transfer after the specific binding of [Fe(CN)6]4- to oxyMb in the His 119(GH1) region, thus catalyzing the protein oxidation.
A stranded juvenile fin whale was successfully euthanized with an intravenous injection of sedative and cardioplegic drugs. Veterinarians may face a number of serious difficulties if called to perform this task, and advance preparation is required for successful euthanasia of these animals.
X-ray scattering curves for the sperm whale myoglobin molecule and a model which includes only the helical regions of the polypeptide chain are calculated. The portion of the scattering curve associated with the packing of the helices inside the protein globule is analyzed. The model of the myoglobin molecule is used to investigate the sensitivity of the scattering curve to changes in the mutual packing of the helical regions.
The heme derivative 2,4-diacetyldeuterohemin deuterated in the methyl groups of the acetyl moieties was reconstituted with sperm whale apomyoglobin and the two labeled methyl groups in the protein environment were observed by deuterium nuclear magnetic resonance spectroscopy. The results were compared to the free hemin form as the dimethyl ester in chloroform and in a pyridine-water mixture, as well as in the zinc complex form. Under most conditions the two methyl resonances overlie each other to a large degree. Resonance width at half-height is of the order of 25 Hz for the protein and approximately one-third as much for the free hemin at 16 degrees and is little affected by conversion to paramagnetic derivatives. Chemical shifts for the oxy- and carbonmonoxymyoglobins are very similar. In cyanoferrimyoglobin a positive pseudo-contact contribution of 3.04 ppm was computed to explain a relative upfield shift offset in part by a small negative contact shift contribution. The cyanoferrimyoglobin resonance was sensitive to the presence of phosphate buffer as well as to cyclopropane. The aquoferrimyoglobin form shows distinct resonances for the two methyl groups, with the downfield resonance considerably broadened. The expected effects of temperature on chemical shift were observed, the paramagnetic derivatives showing an effect and carbonmonoxymyoglobin showing none. The relaxation behavior was gauged from the line widths and from measurements of spin-lattice relaxation time, T1. The effective rotational correlation time is of the order of 50 ps for the liganded myoglobin forms. The temperature dependence of the line widths may imply an increased retational freedom with increasing temperature. The broadening observed in the aquoferrimyoglobin case is indicative of restricted internal rotational motion of one of the methyl groups. The method is suitable for probing the more mobile structures in proteins and retains its value in the neighborhood of paramagnetic centers.
The Cepsilon methyl group of the 2 methionine residues in sperm whale myoglobin was enriched with respect to 13C. This was accomplished by treatment of the apomyoglobin at pH 4 at room temperature with a 100-fold proportion of 13CH3I to form an intermediate containing enriched S-methylmethionine. Unselective demethylation to regain the apomyoglobin structure was accomplished by treatment at pH 10.5 with 0.5 M dithioerythritol at 37 degrees for 18 h. Reagents were removed at each stage by dialysis against dilute sodium azide solution. Hemin was reincorporated to form the holoprotein in a way that avoided the presence of an excess of the small molecule. After chromatographic purification the enriched myoglobin was obtained in a yield of between 29 and 60%. The composition, absorbance spectrum, circular dichroism spectrum, isoionic point, electrophoretic behavior, and oxygen-binding behavior following reduction were all indistinguishable from those of the virgin protein. NMR measurements were made at 15.1, 25.2, and 67.9 MHz at 27-30 degrees. The two enriched loci are represented by separate resonances that appear slightly downfield of the spectral position of the corresponding resonance in free methionine. The positions of these resonances are sensitive to pH and to the ligand bound at the heme group which is approximately 17 A distant from each methionine Cepsilon. On the basis of two separate types of experiment the downfield resonance was assigned to methionine 55 and the upfield resonance to methionine 131. Part of the observed variations in chemical shift could be treated as arising from pseudocontact interactions but part was ascribed to structural changes communicated to the environment of each methionine residue as a result of changes in heme ligand, pH, or temperature. The linewidths of the methionine Cepsilon resonances are narrowed by increasing temperature according to an Arrhenius energy of activation of nearly 3 kcal. The spin-lattice relaxation times, T1, of the two methionine Cepsilon resonances at the three spectrometer frequencies were interpreted to indicate the existence of rotational motions in each side chain in addition to that about the Sdelta-Cepsilon bond. The results as a whole show that the two methionine side chains undergo continuous variations in environment, and that these variations are controlled by events at a distance within the protein structure. It is suggested that the structural lability serves the function of facilitating conformational variations and adjustments within the heme pocket.
Botulism is a neuroparalytic illness caused by toxins produced by the bacterium Clostridium botulinum, an obligate anaerobe found commonly in the environment. Intoxication with toxin type E is associated exclusively with eating animal foods of marine (salt or fresh water) origin. Persons who eat raw or fermented marine fish and mammals are at high risk for botulism from type E toxin. On July 17, 2002, the Alaska Division of Public Health investigated a cluster of suspected botulism cases among residents of a fishing village in Alaska. This report summarizes the findings of the outbreak investigation, which linked disease to eating raw muktuk (skin and a pink blubber layer) from a beached whale (Figure). To avoid delays in treatment, health-care providers evaluating patients suspected of having botulism should base treatment decisions on clinical findings. Public health authorities should be notified immediately about any suspected botulism case.
The functional properties of hemoglobin from the whale Balaenoptera acutorostrata have been characterized as a function of pH, CO2, organic phosphates and temperature. Carbon dioxide effect does not depend on the presence of organic phosphates such as 2,3-DPG and P6-inositol while it is strongly affected by temperature, so that at 37 degrees C it is completely abolished. This, together with the very small delta H of oxygen binding (delta H = -4 to -2 Kcal/mol of oxygen at pH 7.4) has been physiologically interpreted on the basis of the specific metabolic needs of fins and tail which are the place of a great muscular activity.
Site-directed mutants of sperm whale myoglobin were prepared to probe the functional role of the highly conserved distal pocket valine residue, Val68(E11). This amino acid was replaced with Ala, Ile, and Phe to examine the effects of the side chain volume at position 68 on ligand binding. Three double mutants were also constructed in which the distal His64(E7) was replaced with Gly and Val68 was replaced with Ala, Ile, and Phe to determine the effects of size at position 68 in the absence of the distal histidine. Association and dissociation rate constants for O2, CO, and alkyl isocyanide binding were measured by stopped-flow rapid mixing, conventional flash, and laser photolysis techniques at pH 7, 20 degrees C. The association rate constants for the binding of all eight ligands to the single mutants decreased in the order Ala68 greater than Val68 (native) greater than Ile68 myoglobin, indicating that the 68(E11) residue is part of the overall kinetic barrier. A similar pattern was observed for the association constants of the double mutants: Gly64/Ala68 greater than Gly64/Val68 greater than Gly64/Ile68. Thus, increasing size of the E11 side chain inhibits the rate of ligand binding even in the absence of histidine at position 64. Substitution of Ala for Val68 had little effect on O2 affinity but did increase the affinities for CO and isocyanide binding. The affinities for all of the ligands were decreased for the Ile68 mutant. The ligand binding affinities for the Gly64/Ala68, Gly64/Val68, and Gly64/Ile68 myoglobins displayed an analogous trend to that of the single mutants, indicating that the equilibrium interactions between the position 64 and 68 side chains and the bound ligand are roughly additive. Both the association rate constants and dissociation rate constants for O2 and isocyanide binding were decreased for the Phe68 mutant myoglobin. These kinetic parameters result in little change in O2 affinity and an increase in isocyanide affinity, relative to the native protein. Thus, the large benzyl side chain of phenylalanine at position 68 inhibits the rate of ligand movement up to and away from the iron atom but not the final bound state.
Time courses for NO, O2, CO, methyl and ethyl isocyanide rebinding to native and mutant sperm whale myoglobins were measured at 20 degrees C following 17-ns and 35-ps laser excitation pulses. His64 (E7) was replaced with Gly, Val, Leu, Phe, and Gln, and Val68 (E11) was replaced with Ala, Ile, and Phe. For both NO and O2, the effective picosecond quantum yield of unliganded geminate intermediates was roughly 0.2 and independent of the amino acids at positions 64 and 68. Geminate recombination of NO was very rapid; 90% rebinding occurred within 0.5-1.0 ns for all of the myoglobins examined; and except for the Gly64 and Ile68 mutants, the fitted recombination rate parameters were little influenced by the size and polarity of the amino acid at position 64 and the size of the residue at position 68. The rates of NO recombination and ligand movement away from the iron atom in the Gly64 mutant increased 3-4-fold relative to native myoglobin. For Ile68 myoglobin, the first geminate rate constant for NO rebinding decreased approximately 6-fold, from 2.3 x 10(10) s-1 for native myoglobin to 3.8 x 10(9) s-1 for the mutant. No picosecond rebinding processes were observed for O2, CO, and isocyanide rebinding to native and mutant myoglobins; all of the observed geminate rate constants were less than or equal to 3 x 10(8) s-1. The rebinding time courses for these ligands were analyzed in terms of a two-step consecutive reaction scheme, with an outer kinetic barrier representing ligand movement into and out of the protein and an inner barrier representing binding to the heme iron atom by ligand occupying the distal portion of the heme pocket. Substitution of apolar amino acids for His64 decreased the absolute free energies of the outer and inner kinetic barriers and the well for non-covalently bound O2 and CO by 1 to 1.5 kcal/mol, regardless of size. In contrast, the His64 to Gln mutation caused little change in the barrier heights for all ligands, showing that the polar nature of His64 inhibits both the bimolecular rate of ligand entry into myoglobin and the unimolecular rate of binding to the iron atom from within the protein. Increasing the size of the position 68(E11) residue in the series Ala to Val (native) to Ile caused little change in the rate of O2 migration into myoglobin or the equilibrium constant for noncovalent binding but did decrease the unimolecular rate for iron-O2 bond formation.(ABSTRACT TRUNCATED AT 400 WORDS)