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Titolo:
CELL-WALL ANTIGENS OF PNEUMOCYSTIS-CARINII TROPHOZOITES AND CYSTS - PURIFICATION AND CARBOHYDRATE ANALYSIS OF THESE GLYCOPROTEINS
Autore:
DESTEFANO JA; MYERS JD; DUPONT D; FOY JM; THEUS SA; WALZER PD;
Indirizzi:
VET ADM MED CTR CINCINNATI OH 45220 VET ADM MED CTR CINCINNATI OH 45220 UNIV CINCINNATI,COLL MED,DEPT INTERNAL MED CINCINNATI OH 45267 APPL BIOSYST INC FOSTER CITY CA 94404 UNIV GEORGIA,COMPLEX CARBOHYDRATE RES CTR ATHENS GA 30602
Titolo Testata:
The Journal of eukaryotic microbiology
fascicolo: 3, volume: 45, anno: 1998,
pagine: 334 - 343
SICI:
1066-5234(1998)45:3<334:CAOPTA>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAJOR SURFACE GLYCOPROTEIN; LINKED IMMUNOSORBENT-ASSAY; MONOCLONAL-ANTIBODIES; POLYACRYLAMIDE GELS; RAT; IDENTIFICATION; PNEUMONIA; PROTEINS; MEMBRANE; GENES;
Keywords:
BIOCHEMICAL ANALYSIS; DEVELOPMENTAL STAGES; OPPORTUNISTIC PATHOGEN; STRUCTURE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
67
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Destefano et al., "CELL-WALL ANTIGENS OF PNEUMOCYSTIS-CARINII TROPHOZOITES AND CYSTS - PURIFICATION AND CARBOHYDRATE ANALYSIS OF THESE GLYCOPROTEINS", The Journal of eukaryotic microbiology, 45(3), 1998, pp. 334-343

Abstract

We have purified and biochemically analyzed individual cell wall glycoproteins of Pneumocystis carinii. Our results show that correspondingcore glycoproteins constitute the cell wall antigens in both trophozoites and cysts, and glycosylation of these glycoproteins does not appear to be significantly altered during development. Cysts and trophozoites in rat-derived organism preparations were separated from each other by counterflow centrifugal elutriation, then treated with Zymolyase to obtain the cell wall fractions. Gel electrophoresis patterns of these fractions from both life-cycle stages were qualitatively similar. Ten major antigenic glycoproteins in these fractions were purified by preparative continuous elution gel electrophoresis. All ten glycoproteins from cysts and trophozoites contained mannose, glucose, galactose, and N-acetylglucosamine, and some contained traces of fucose. The glycoproteins of cysts had more mannose than their trophozoite counterparts. The trophozoite glycoproteins differed from those of the cyst by the presence of xylose. To examine the species-specificity of glycoprotein glycosylation, preparations of human-derived P, carinii (comprised of mixed life-cycle stages) were also examined and found to contain the same sugars as those found in rat-derived organisms. Most of the purified rat-derived glycoproteins bound Concanavalin A, which was abolished by treatment with N-glycanase. This suggested that the majority ofthe oligosaccharides were N-linked to the proteins, but attempts to identify carbohydrate linkage sites by amino acid sequencing were hampered by apparent modifications of residues. The peptides derived by cyanogen bromide cleavage revealed distinct size patterns for each glycoprotein, suggesting that they were distinct proteins. Most of the glycoproteins reacted with monoclonal antibodies which recognize a highly conserved epitope on rat P. carinii. Four of the individually purified glycoprotein preparations elicited in vitro cellular immune responses,implicating their involvement in the recognition of P. carinii by host T cells. The identification and characterization of P. carinii cell wall proteins will be helpful in analyzing the relationship of the organism to its mammalian host.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 11/07/20 alle ore 13:20:54