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Chapter 5 : Microsporidian Biochemistry and Physiology

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Abstract:

The microsporidia are a large group of highly specialized obligate intracellular protozoan parasites. Disturbances in the biochemical composition of tissues infected by intracellular parasites are of interest because such infections often significantly alter the electrolyte, carbohydrate, protein, and free amino acid pools of host cells. Until recently, biochemical investigations of the metabolic processes of the microsporidia have suffered because of insufficient numbers of the different parasite stages and inadequate methods for the in vitro cultivation and maintenance of these organisms. The authors have observed the disappearance of glycogen granules in the host cell cytoplasm during the early stages of parasite development without any concomitant change in the size or quantity of lipid droplets. The microsporidian species is a model for investigating externally mediated signal transduction and subsequent activation of the internal signal pathway for triggering of a missile cell, the microsporidian spore. Microsporidian meront stages appear to have actin-myosin and kinesin-associated molecular motors. This chapter focuses on keratin filaments found in two domains: (i) within the spore stage, the microsporidian sporophorous vesicle, and (ii) keratin in the host cell cytoplasm domain but situated at its interface with the parasite. Recently, however, some success has been achieved in isolating and maintaining meronts and discharged sporoplasms in extracellular support medium. Developing a simple in vitro model will be useful for many subsequent biochemical analyses.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5

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Small Nuclear RNA
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Intermediate Filament Protein
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Figures

Image of FIGURE 1
FIGURE 1

Effect of infection on the skeletal muscle composition of the blue crab (). Data are presented as the percentage difference in protein, free amino acid (NPS), and carbohydrate (CHO) levels of thoracic versus cheliped skeletal muscle. Bar direction indicates whether values for thoracic muscle were higher (+) or lower (-) than those for cheliped muscle (mean ± 95% confidence interval).

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 2
FIGURE 2

Lactate concentrations in the hemolymph, thoracic skeletal muscle, and hepatopancreas of normal, lightly infected, and heavily infected blue crabs (mean ± 95% confidence interval).

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 3
FIGURE 3

Glucose utilization, lactate production, and pyruvate production by isolated sporoplasms incubated in medium 199 containing 5.5 mM glucose. Data are presented as (cumulative) micromoles of solute per 10 sporoplasms (mean ± 95% confidence interval).

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 4
FIGURE 4

Uptake of U-C-D-glucose by isolated sporoplasms. Data are presented as micromoles of glucose taken up per 10 sporoplasms. Incubations in low-substrate (minimum essential medium, 0.5 mM glucose) and high-substrate (medium 199, 5.5 mM glucose) media are compared (mean ± 95% confidence interval).

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 5
FIGURE 5

A proposed scheme of energy metabolism in microsporidian spores.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 6
FIGURE 6

Polarographic measurement of oxygen consumption by mitochondria isolated from a (Lepidoptera: Noctuidae) fat body infected with

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 7
FIGURE 7

Surface topography of the outer envelope surrounding spores. (A) Platinum-shadowed spore with the outer envelope partially dispersed after preincubation in urea and a rinse in distilled water. Arrows indicate envelope is compartmentalized. (B) Isolated spore envelope stained with phosphotungstic acid. Arrows indicate compartments with internal matrix which probably buffer proteins within these domains. (C) Isolated spore envelope stained with uranyl acetate. Visualized proteins (arrows) are weakly stained within the compartments so clearly delineated in panel B. The compartmental channels are 75 to 100 nm in width.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 8
FIGURE 8

Immunoblot analyses of spore envelope proteins specific for G protein (α-subunits). Antisera GC/2 recognizes Goα (lanes 1 and 2); CO/1 recognizes Goα and Giα 3 (lanes 3 and 4) and RM/1 is specific for Gsα (lanes 5 and 6). For controls, rat brain membrane proteins are in lanes 2, 4 and 6, and envelope peptides are in lanes 1, 3 and 5.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 9
FIGURE 9

spore envelope isolate. (A) Uranyl acetate-stained proteins partially isolated from spore envelope but still in the native linear arrangement (arrows). (B) Isolate of envelope with proteins tested against anticlathrin and reacted with a second antibody coupled to peroxidase. Arrows indicate peroxidase reaction is limited to threadlike elements. Magnification, × 200,000.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 10
FIGURE 10

spore polar aperture area. Arrows indicated precipitate that frequently accumulated near spore aperture after CaCl incubation. Since precipitation was confined to this site, one assumption is that the calcium salt accumulates here because of the channel proteins at this aperture (where the Cainflux is believed to occur). Magnification, × 200,000.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 11
FIGURE 11

Nucleotidase activity in the isolated spore envelope of . The envelopes were incubated in nitrophenyl phosphate or ATP (1 mM), and the substrate was incubated in medium with the capture agent cerium. The cytochemical medium contained 0.1 M Tris-maleate (pH 7.4), CeCl, ATP, or nitrophenyl phosphate (Robinson and Karnovsky, 1983). Reaction was confined to the envelope channels. Magnification, × 35,000.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 12
FIGURE 12

The presumed anatomy of a sporophorous vesicle with keratin and plaque proteins. The arrow indicates the position of the jacket assemblage (bearing the keratin) that envelops the spore. The evidence for channel continuity with the vesicle exterior is indicated by the permeation of lanthanum and dyes into the area between the jacket and the spores; no probe material penetrated the primary space between the jacket and the vesicle envelope.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 13
FIGURE 13

Electron micrograph showing spore colony removed from host neuron after 6 h in culture medium. Filament bundles still persist and comprise the matrix between the spores or meronts and hold these cells together. Magnification, ×30,000.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 14
FIGURE 14

Images of sporoplasms in extracellular culture media. (A) Phase light micrograph of sporoplasms after 12 h in medium. (B) Electron micrograph of sporoplasms. Arrows indicate apparent interiorizing on surface of cell. (C and D) DAPI-stained sporoplasms after 24 h in culture. Arrows indicate presumptive divider cells. (E) Sporoplasms after 10-min incubation in rhodamine-albumin with some accumulation of label in small fluorescent domains at the surface (arrows). (F and G) DAPI-stained sporoplasms after 24 h in culture. Arrows show a cell in apparent division. (H and I) Sporoplasms incubated for 20 min in dextran. Arrows point to vacuoles as possible sites of dextran endocytosis. Sporoplasms are 2 μm in diameter.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Image of FIGURE 15
FIGURE 15

The periphery of an isolated extracellular meront colony after 6 h in culture medium. Cells at the border of the colony (seen here) were apparently in better physical condition than interior cells of the colony, indicating that the dense matrix between meronts may affect nutrient infiltration. Magnification, X25.000.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
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Tables

Generic image for table
TABLE 1

Activities of enzymes in microsporidian spores

Figure in parentheses indicates the number of separate spore purification procedures.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5
Generic image for table
TABLE 2

Activities of enzymes in the fat body of control and infected crickets ()

Figure in parentheses indicates the number of independently examined crickets.

Citation: Weidner E, Findley A, Dolgikh V, Sokolova J. 1999. Microsporidian Biochemistry and Physiology, p 172-195. In Wittner M, Weiss L (ed), The Microsporidia and Microsporidiosis. ASM Press, Washington, DC. doi: 10.1128/9781555818227.ch5

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