Serum protein electrophoresis by using high-resolution agarose gel in clinically healthy and Aspergillus species-infected falcons.
Key words: aspergillosis, serum protein electrophoresis, high-resolution agarose gel, prealbumin, avian, falcons, Falto species, Falconidae
Evaluation of blood protein distribution by electrophoresis allows the early detection of inflammatory and humoral responses, and is a well-established aid to the diagnosis of many diseases of humans and animals. (1) Protein electrophoresis has gained importante in avian medicine during the past decade, (1) and it has become evident that interpretation of patterns should be based on species-specific reference intervals because of differences in fractions among different avian species. (2) Several attempts have been made to establish reference intervals for various bird species and electrophoretic patterns for common avian diseases. (2-5) However, lack of data for many bird species and inconsistency in methodology and interpretation make it difficult for clinicians to include protein electrophoresis as part of routine diagnostic procedures in birds. Currently, diagnostic confirmation of aspergillosis in birds relies on endoscopy and cytologic examination or fungal culture of air sac biopsy samples. (6) In addition, protein electrophoresis is a useful adjunct diagnostic tool to detect changes in blood proteins, potentially indicating the acute phase of a disease process at an early stage as well as monitoring recovery and the success of therapy. (7)
The aim of this study was to evaluate results of serum protein electrophoresis (SPE) in falcons commonly used in falconry in the Middle East, to develop reference intervals, and to examine the diagnostic validity in cases of aspergillosis. Results of SPE from falcons with confirmed aspergillosis were analyzed and compared with results from clinically healthy birds.
Materials and Methods
Serum protein electrophoresis was performed on blood samples collected from 105 falcons that were submitted to the Dubai Falcon Hospital (Dubai, United Arab Emirates) between 2003 and 2006. The species of falcons from which samples were obtained were peregrine falcons (Falco peregrinus), gyrfalcons (Falco rusticolus), saker falcons (Falco cherrug), red-naped shaheens (Falco pelegrinoides babylonicus), and gyr-hybrid falcons (gyrfalcon x peregrine falcon, gyrfalcon x saker falcon, gyrfalcon x red-naped shaheen). The falcons were categorized into 2 groups: group 1, clinically healthy birds (n = 73), and group 2, birds with confirmed aspergillosis (n = 32). The number, species, and sex of the falcons in the 2 groups are listed in Table 1.
Health checks were performed on all falcons presented to the Dubai Falcon Hospital for prepurchase examinations or because of sickness. Clinical status was assessed by selective diagnostic procedures that comprised physical examination, parasitologic screening for endoparasites (microscopic examinations of feces and a crop swab), hematologic testing, whole-body radiographs (ventrodorsal and lateral views), endoscopic examination of the air sacs, and examination of biopsy samples or swabs taken during diagnostic procedures by cytologic examination, mycotic culture, or both, and by aerobic bacterial culture.
The falcons were categorized as clinically healthy (group 1) when no abnormalities were found during physical, hematologic, endoscopic, and radiographic examinations. Birds with positive parasitologic findings were only included if they were asymptomatic.
Birds included in group 2 were considered infected with Aspergillus species if macroscopic changes of the trachea and the lower respiratory tract, including lungs and air sacs, were apparent during endoscopic examination and Aspergillus species was isolated from a biopsy sample of air sac lesions or if results of cytologic examination of air sac biopsy samples were consistent with mycotic infection. Samples were cultured in Sabouraud chloramphenicol agar and incubated at 37[degrees]C (98.6[degrees]F) for 3-5 days. Fungi were identified by culture appearance and morphologic characteristics determined by microscopic examination of specimens prepared by lactophenol aniline stain.
Blood samples were collected from the vena metatarsalis medialis or vena basilica and transferred into 1-mL serum gel separation tubes (Sarstedt, Nuembrecht, Germany). Serum tubes were kept in a tube rack for 1-3 hours at room temperature (23[degrees]C [73.4[degrees]F]) for clot formation, then subsequently centrifuged at 2332g for 5 minutes (Micromax IEC, Needham Heights, MA, USA). Separated serum samples were stored at -80[degrees]C (-110[degrees]F) until analysis (up to 2 years). Hemolyzed samples were removed from the study. Total protein (TP) and albumin concentrations were determined in an automated chemistry analyzer (Mira Plus, Montpellier, France) by the biuret and bromocresol green (BCG) dye-binding method, respectively. Spintrol bovine control samples were used in each day of analysis according to the manufacturer's protocol (Spin-react, Sant Esteve de Bas, Spain).
Serum protein electrophoresis
Electrophoresis was performed in a SAS 1 unit (Helena, Saint Leu La Forest, France) with 2 applications at an electric voltage of 100 V for 18 minutes by using a high-resolution agarose gel (SAS-1 SP-24 SB; Helena). The staining procedure was done by using an auto stainer SAS 2 (Helena). The gel images were scanned by using an Epson Perfection 3170 photo scanner (Hirooka Shiojiri-Shi, Nagano-Ken, Japan) and were read with platinum gel analysis software (Helena). Normal and abnormal Kemtrol serum controls (Helena) were used in each run of electrophoresis.
[FIGURE 1 OMITTED]
In this study, peaks in the electrophoretogram were assigned to the different protein fractions based on the albumin value obtained by the BCG method. Once the albumin peak was identified in the electrophoretogram, further peaks were assigned to the main groups of globulin fractions according to their migration distance and regardless of any further subdivision. The albumin:globulin (A:G) ratio was calculated as the following: (prealbumin + albumin)/(alpha + beta + gamma globulins). (2)
Statistical analysis was performed by using SigmaPlot 11.0 (Systat Software Inc, Erkrath, Germany), Reference intervals were calculated by using MedCalc 126.96.36.199 (Medcalc Software bvba, Marienkerke, Belgium). Normality was assessed with the Kolmogorov-Smirnov statistic. If the data were not normally distributed, then nonparametric tests were applied (Mann-Whitney U test, Kruskal-Wallis test). To investigate the correlation between the albumin values obtained by the BCG method and SPE, a least squares regression line was fitted to the data (Fig t). Significance was set at P < .05.
In both groups, only the values of albumin determined with BCG and the A:G ratio were normally distributed according to the Kolmogorov-Smirnov test (Table 2). Values, therefore, were also expressed by the median and the interquartile range. A comparison of results between groups 1 and 2 was performed by using the unpaired t test in the case of normally distributed data and by using the Mann-Whitney U test with nonparametric data, respectively. Reference intervals were calculated by using the "robust method" for smaller sample sizes (fewer than 120) as recommended by the National Committee on Clinical Laboratory Standards and Clinical and Laboratory Standards Institute guidelines C28-A2 and C28-A3 for estimating percentiles ([P.sub.2.5] - [P.sub.97.5]) and their 90% confidence intervals (Table 2). (8)
The data from clinically healthy birds (group 1) were evaluated for differences among different species and between sexes by using analysis of variance and the unpaired t test for normally distributed data and the Kruskal-Wallis test and the Mann-Whitney U test in cases in which normality failed.
Thirteen birds in group 1 had positive parasitologic findings in feces and crop swabs but were asymptomatic. Findings were Caryospora megafalconis (n = 1), Serratospiculum species (n = 10), Pseudostrigea falconis (n = 1), Trichomonas species (n = 3), and Capillaria species (n = 1). Albumin values for group 1 and group 2 birds obtained by the BCG method and by SPE were highly correlated (Fig 1). Based on calculations of TP and the albumin fraction obtained by the biuret method and the BCG method, respectively, 5 protein fractions were identified in the electrophoretogram: prealbumin, albumin, alpha globulin, beta globulin, and gamma globulin (Fig 2). In 4 electrophoretograms (1 bird from group 1 and 3 birds from group 2), the high-resolution agarose gel (SAS-1 SP-24 SB) produced a twin peak in the alpha-globulin fraction.
No significant differences were found in values for A:G ratios and protein fractions among the different species or between sexes. The SPE values for peregrine, gyr, saker, hybrid falcons, and red-naped shaheens, therefore, were combined for all falcon species (Table 2). Evaluation of the protein fraction values revealed significant differences between group 1 and group 2 for albumin concentrations determined by the BCG method, total albumin concentration (albumin + prealbumin), and prealbumin (Table 2). An example of differences in the SPE pattern in a clinically healthy bird compared with a bird with confirmed aspergillosis is illustrated in Figure 3.
One of the most striking findings in this study was a high double peak within the albumin fraction in the SPE pattern, of which the first one was assigned to prealbumin. Interestingly, prealbumin was one of the values significantly different between clinically healthy and aspergillosis birds. Prealbumin serves as a carrier for various transport proteins and acts as a negative acute-phase protein, which may explain its decline in aspergillosis-affected birds in this study. (9,10) Prealbumin fractions are usually negligible in mammalian species. (9) In birds, however, prealbumin can represent from 10% to 75% of the total albumin fraction, depending on the species of birds. (2-5,11,12) The inconsistent prealbumin values are thought to be a function of technique and electrophoresis apparatus because some conditions may cause the loss of these rapidly migrating molecules, 11-14 which could be confirmed in a pilot study (Fig 4) in which prealbumin fractions were not apparent in 63% of the samples or could not be read properly because of their fast migration in the agarose standard gel (SAS-1 SP-24 gel). In comparison, 95% of the samples showed clear prealbumin fractions when using a high-resolution agarose gel (SAS-1 SP-24 SB gel). The presence of prealbumin is also believed to depend on the species, as has been demonstrated in several psittacine species when using the same method. (15) In addition, physiologic status of the bird may play a role: variable occurrence of prealbumin was reported in laying hens, (16) however, the occurrence of prealbumin was not associated with seasonality in female birds in our study, and differences in prealbumin values showed no correlation to molting or egg formation as shown in other bird species. (4)
Compared with results of previous studies, (3,17) this study revealed relatively low TP values for falcons, along with high values for prealbumin and for the A :G ratio. Likewise, high values for prealbumin were previously found for Spanish imperial eagles (Aquila adalberti). (12) The A: G ratio is a primary indicator from the protein electrophoresis. In some cases of immune response, TP may remain within the normal range, but the shift of protein fractions and resultant change in A:G ratio have more clinical significance than the TP alone. (2,11,18) However, as a natural response to physiologic situations, such as egg laying or migration, (1) season, age and husbandry, (5) and pathologic conditions in general, protein levels are not exclusively related to certain diseases and should always be interpreted in relation with other diagnostic measures. In our study, variability in SPE patterns between different sexes was not statistically significant for healthy falcons (n = 73), which was in agreement with previous studies, according to which reference values appear to be significantly different among different genera but negligible among taxonomic species. (3,15,17,19)
[FIGURE 2 OMITTED]
[FIGURE 3 OMITTED]
[FIGURE 4 OMITTED]
Published protein electrophoretic patterns in birds are diverse and often inconsistent because of insufficient information about standardized methods of defining the different protein fractions. (2,18) A recent study questions the reliability of the determination of alpha, beta, and gamma globulins by protein electrophoresis in birds in particular and offers some explanations for the variations of the globulin fraction values, such as low sample volumes for globulin fractions, technical variations in the methodology, and limitations of the statistical methods. (13,20) The identification of the different protein fractions in the electrophoretogram in the current study was based on albumin values obtained by the BCG method. Although this method showed poor correlation to electrophoretic albumin values determined by cellulose acetate membrane in pigeons (Columba livia), (21) it provided us, based on the strong correlation between the 2 methods in this study, an approximation of the albumin value. Starting from the identification of the albumin peak, the band with a faster migration than albumin, if present, was assigned to prealbumin and the 3 bands with slower migration were assigned to the main groups (alpha, beta, gamma) of globulins. These assumptions were confirmed in a small pilot study by the obvious elevation of one peak in the electrophoretogram pattern of plasma compared with serum, which likely represents fibrinogen in the beta-globulin fraction (Fig 2). The identification of additional protein subfractions, such as [alpha.sub.1]- and [alpha.sub.2]-globulins, or twin peaks in beta-globulin have been reported in different bird species. (2,3,11) In this study, the high-resolution agarose gel (SAS-1 SP-24 SB) produced a twin peak in the alpha-globulin fraction in only 4 electrophoretograms (1 bird from group 1 and 3 birds from group 2), which could not be further explained. Ina recent study, in which the investigators used de novo sequencing to define the protein fractions more precisely, the [alpha.sub.1]-globulin peak was identified as apolipoprotein A-I, (22) which underlines the importance of clearly describing the methods of identifying the protein fractions in the electrophoretogram until more specific studies (eg, immunoelectrophoresis (2)) are performed.
In contrast to many other studies on protein electrophoresis in birds, serum was used instead of plasma because fibrinogen in plasma samples can obscure the electrophoretogram in the beta- and gamma-globulin regions, (23) and heparin may interfere with BCG dye, (21,24) which precludes reliable albumin measurements. Because serum separates from the blood clot and is in contact with blood cells for a longer time than in plasma samples that are usually immediately centrifuged, it inevitably undergoes changes due to continuing metabolic activities and, therefore, is not recommended for obtaining blood biochemical values. Because cellular metabolism has not been reported to change protein fractions, serum was thought to be more advantageous for protein electrophoresis. However, when interpreting electrophoretic patterns, one should be aware that TP is lower in serum than in plasma and that peaking of the beta-globulin fraction may not be as prominent because of the missing acute-phase protein fibrinogen. (25) The lack of fibrinogen in serum samples of this study coupled with the relatively high values of prealbumin may explain the comparably high A : G ratios. Potential limitations of this study are the lack of comparison of paired plasma and serum samples of the same birds to clarify the influence of fibrinogen.
In most studies, birds with clinical aspergillosis show increased total blood protein concentrations, marked hyperglobulinemia (beta and gamma fraction), and decreased albumin fraction that resulted in a decreased A:G ratio. (2,3,11,26) In fact, in penguins, a connection among albumin levels that dropped below 0.18 mg/dL and poor prognosis was shown, (27) and, compared with antigen and antibody enzyme-linked immunosorbent assays, protein electrophoresis showed the highest sensitivity. (26) In some individual cases, these changes could also be seen in this study (Fig 3); however, apart from the decreased total albumin concentration determined by SPE, the results were not significantly different between groups 1 and 2. However, in most of these studies, plasma was used, and the increase in the beta region likely originated from increased fibrinogen, which could not be observed in the current study because of the use of serum. Another explanation for this may be that birds presented to Dubai Falcon Hospital are trained falconry birds; these birds are closely observed by their trainers every day and changes in performance are noticed in very early stages of disease.
Because abnormal electrophoretic patterns may precede seroconversion, detection of pathogens, or biochemical and hematologic values, (1-3,28) SPE can be used as an accessory tool to indicate pathologic conditions in falcons, for example, aspergillosis. In particular, a decrease in the prealbumin fraction may be an important early indicator; however, further investigations are necessary to identify the appropriate standardized methods to distinctively identify the electrophoretographic fractions and elucidate the significance of this potential negative acute phase protein in the diagnosis of aspergillosis in birds.
Acknowledgments: We thank His Highness Sheikh Hamdan bin Rashid al Maktoum for his continued support of the Dubai Falcon Hospital. We thank Mr Humaid Obaid al Muhari and the staff of the Dubai Falcon Hospital for their technical support. We thank Dr Donatella Gelli for her expertise.
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Maya Kummrow, Dr Med Vet, DVSc, Dipl ACZM, Christudas Silvanose, BMLT, Antonio Di Somma, Med Vet, SMPA, Thomas A. Bailey, BVSc, MRCVS, MSc, PhD, CcrtZooMed, Dipl ECAMS, and Susanne Vorbruggen, Med Vet
From the Zoo Hannover GmbH, Adenauerallee 3, 30175 Hannover, Germany (Kummrow); the Dubai Falcon Hospital, PO Box 23919, Dubai, United Arab Emirates (Silvanose, Di Somma, Bailey); Aviculture and Health, International Wildlife Consultants, PO Box 19, Carmarthen, Dyfed, Wales, SA33 5YL United Kingdom (Bailey); and the Klinik fur Vogel und Reptilien, Universitat Leipzig, An den Tierkliniken 17, 04103 Leipzig, Germany (Vorbruggen).
Table 1. Distribution of species, health status and sex of the 105 falcons of the study. Falcon species Group (a) Males Females Total Peregrine (n = 26) 1 11 14 25 2 0 1 1 Saker (n = 10) 1 0 6 6 2 0 4 4 Gyrfalcon (n = 22) 1 2 12 14 2 4 4 8 Red-naped shaheens (n = 3) 1 0 3 3 2 0 0 0 Hybrid falcons (n = 44) 1 7 18 25 2 5 14 19 Total group 1 20 53 73 Total group 2 9 23 32 Total both groups 29 76 105 Abbreviation: n indicates sample size. (a) Group 1 are clinically healthy falcons; group 2 are falcons with confirmed aspergillosis. Table 2. Serum protein values (g/dL) for clinically healthy falcons (group 1) and for falcons with confirmed aspergillosis (group 2). Variable Mean (SD) 95 % CI Group 1 (n = 73) TP, g/dL (biuret) 3.18 [+ or -] 1.78 2.77-3.60 Albumin, g/dL (BCG) (a) 1.14 [+ or -] 0.48 0.10-1.28 A : G ratio (a) 1.36 [+ or -] 0.37 0.48-2.24 Total albumin, g/dL 1.74 [+ or -] 0.80 1.55-1.93 Prealbumin, g/dL (SPE) 0.68 [+ or -] 0.32 0.60-0.75 Albumin, g/dL (SPE) 1.08 [+ or -] 0.53 0.9.6-1.21 Alpha globulin, g/dL (SPE) 0.48 [+ or -] 0.42 0.38-0.58 Beta globulin, g/dL (SPE) 0.45 [+ or -] 0.25 0.39-0.50 Gamma globulin, g/dL (SPE) 0.53 [+ or -] 0.49 0.41-0.64 Group 2 (n = 32) TP, g/dL (biuret) 2.66 [+ or -] 1.57 2.10-3.23 Albumin, g/dL (BCG) 0.92 [+ or -] 0.52 0.73-1.11 A : G ratio (a) 1.22 [+ or -] 0.54 1.02-1.42 Total albumin, g/dL 1.32 [+ or -] 0.76 1.04-1.59 Prealbumin, g/dL (SPE) 0.43 [+ or -] 0.34 0.29-0.56 Albumin, g/dL (SPE) 0.93 [+ or -] 0.52 0.75-1.12 Alpha globulin, g/dL (SPE) 0.44 [+ or -] 0.40 0.30-0.59 Beta globulin, g/dL (SPE) 0.42 [+ or -] 0.33 0.30-0.54 Gamma globulin, g/dL (SPE) 0.49 [+ or -] 0.42 0.34-0.64 Interquartile Variable Median range Group 1 (n = 73) TP, g/dL (biuret) 2.7 2.20-3.93 Albumin, g/dL (BCG) (a) 1.2 0.70-1.50 A : G ratio (a) 1.43 1.14-1.60 Total albumin, g/dL 1.59 1.23-2.14 Prealbumin, g/dL (SPE) 0.65 0.49-0.82 Albumin, g/dL (SPE) 0.99 0.73-1.23 Alpha globulin, g/dL (SPE) 0.39 0.29-0.54 Beta globulin, g/dL (SPE) 0.36 0.31-0.52 Gamma globulin, g/dL (SPE) 0.37 0.26-0.59 Group 2 (n = 32) TP, g/dL (biuret) 2.4 1.65-3.05 Albumin, g/dL (BCG) 0.88 0.56-1.18 A : G ratio (a) 1.14 0.78-1.61 Total albumin, g/dL 1.24 0.87-1.52 Prealbumin, g/dL (SPE) 0.34 0.22-0.53 Albumin, g/dL (SPE) 0.83 0.63-1.12 Alpha globulin, g/dL (SPE) 0.28 0.21-0.54 Beta globulin, g/dL (SPE) 0.34 0.19-0.48 Gamma globulin, g/dL (SPE) 0.33 0.24-0.52 Reference Variable interval P value Group 1 (n = 73) TP, g/dL (biuret) 0-6.46 Albumin, g/dL (BCG) (a) 0.14-2.12 A : G ratio (a) 0.63-2.15 Total albumin, g/dL 0-3.22 Prealbumin, g/dL (SPE) 0-1.27 Albumin, g/dL (SPE) 0-2.03 Alpha globulin, g/dL (SPE) 0-1.22 Beta globulin, g/dL (SPE) 0-0.91 Gamma globulin, g/dL (SPE) 0-1.38 Group 2 (n = 32) TP, g/dL (biuret) .06 Albumin, g/dL (BCG) .03 (b) A : G ratio (a) .14 Total albumin, g/dL .002 (b) Prealbumin, g/dL (SPE) <.001 (b) Albumin, g/dL (SPE) .09 Alpha globulin, g/dL (SPE) .12 Beta globulin, g/dL (SPE) .17 Gamma globulin, g/dL (SPE) .42 Abbreviations: CI indicates confidence interval; TP, total protein; A : G, albumin: globulin; BCG, bromocresol green; SPE, serum protein electrophoresis. SI conversion factor: To convert g/dL to g/L, multiply by 10. (a) Normally distributed (Kolmogorov-Smirnov test). (b) Statistically significant (P < .05).
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|Title Annotation:||Original Studies|
|Author:||Kummrow, Maya; Silvanose, Christudas; Di Somma, Antonio; Bailey, Thomas A.; Vorbruggen, Susanne|
|Publication:||Journal of Avian Medicine and Surgery|
|Date:||Dec 1, 2012|
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