Cell-surface sialoglycoconjugate structures in wild-type and mutant Crithidia fasciculata

Cell-surface sialoglycoconjugate structures in wild-type and mutant Crithidia fasciculata

The cell-surface expression of sialoglycoconjugate structures in wild-type Crithidia fasciculata and its TFR(R1) drug-resistant mutant was analyzed with the aid of an influenza C virus strain, lectin, enzymatic treatment, and flow cytofluorimetry analysis probed with fluorescein isothiocyanate-label...

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Published in:Parasitology research (1987) Vol. 85; no. 4; pp. 293 - 299
Main Authors: DO VALLE MATTA, M. A, SALE SALVIANO, D, DOS SANTOS SILVA COUCEIRO, J. N, LEAL MEIRELLES, M. N, SALES ALVIANO, C, ANGLUSTER, J
Format: Journal Article
Language:English
Published: Berlin Springer 01-04-1999
Subjects:
Animals
Biological and medical sciences
Crithidia fasciculata - chemistry
Crithidia fasciculata - genetics
Crithidia fasciculata - metabolism
Drug Resistance
Flow Cytometry
Fundamental and applied biological sciences. Psychology
Gammainfluenzavirus - metabolism
Glycoconjugates - analysis
Glycoconjugates - metabolism
Hemagglutinins - metabolism
Life cycle. Host-agent relationship. Pathogenesis
Neuraminidase - metabolism
Peanut Agglutinin - metabolism
Protozoa
Sialic Acids - analysis
Sialic Acids - metabolism
Kinetoplastida
Protozoa
Life history
Flagellum
Parasite
Crithidia fasciculata
Wild animal
Glycoconjugate
Gene expression
Cell surface
Strain
Sialoglycoproteins
Antibiotic
Sensitivity resistance
Mutation
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Summary:The cell-surface expression of sialoglycoconjugate structures in wild-type Crithidia fasciculata and its TFR(R1) drug-resistant mutant was analyzed with the aid of an influenza C virus strain, lectin, enzymatic treatment, and flow cytofluorimetry analysis probed with fluorescein isothiocyanate-labeled (FITC) lectins. 9-O-Acetyl-N-acetyl neuraminic acid (Neu5,9Ac2) structures mediate influenza C virus cell-binding. The SAalpha2,3Gal and SAalpha2,6Gal sequences are specifically recognized by Maackia amurensis (MAA) and Sambucus nigra (SNA) lectins, respectively. On the basis of these parameters the TFR(R1) mutant strain of C. fasciculata was found to contain exposed sialoglycoconjugates bearing Neu5,9Ac2 surface structures. After the removal of sialic acid residues by neuraminidase activity the marked increases in PNA (peanut agglutinin)-mediated agglutinating activity showed that those acidic units on C. fasciculata cells were glycosidically linked to D-galactose. The bond involves SAalpha2,6Gal and SAalpha2,3Gal linkages as suggested by the use of FITC-SNA and FITC-MAA lectins, respectively. Both SAalpha2,3Gal and SAalpha2,6Gal sequences were preferentially expressed by the TFR(R1) mutant. The SAalpha2,6 linkage markedly predominated. In the TFR(R1) mutant, but not in wild-type cells, two distinct populations of cells were distinguished by reactivity with FITC-SNA, one of which was enriched with surface SAalpha2,6Gal sequences. These diverse findings suggest that sialoglycoconjugate structures present on the flagellate surface may be associated with mutation and the cell growth cycle in C. fasciculata.
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ISSN:0932-0113
1432-1955
DOI:10.1007/s004360050551