[47] O-sialoglycoprotease from Pasteurella haemolytica

Mellors, Alan; Lo, Reggie Y.C.

doi:10.1016/0076-6879(95)48049-8

Cited by 40 publications

(45 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…As its name suggests, it is a neutral metalloprotease which has high specificity for O-sialoglycoproteins attached to serine or threonine residues, most of which are membrane proteins. Substrates include human GPA, CD34, CD43, CD44, and CD45; ligands for P-and L-selectins; tumor antigen epitectin; vascular adhesion protein VAP-1; platelet glycoprotein Ib; and cranin, a brain O-sialoglycoprotein (18). The best-characterized substrate is the transmembrane cell surface glycoprotein of human erythrocytes, GPA (18).…”

Section: Discussionmentioning

confidence: 99%

“…Substrates include human GPA, CD34, CD43, CD44, and CD45; ligands for P-and L-selectins; tumor antigen epitectin; vascular adhesion protein VAP-1; platelet glycoprotein Ib; and cranin, a brain O-sialoglycoprotein (18). The best-characterized substrate is the transmembrane cell surface glycoprotein of human erythrocytes, GPA (18). Although it cannot be the physiological substrate for R. anatipestifer sialoglycoprotease, it was used to determine hydrolysis by Cam, as few glycoproteins from avian target cells are available for testing as potential in vivo substrates.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

et al. 2002

View full text Add to dashboard Cite

Riemerella anatipestifer is responsible for exudative septicemia in ducks. The genetic determinant of the CAMP cohemolysin, cam, from a strain of R. anatipestifer was cloned and expressed in Escherichia coli. Chromosomal DNA from serotype 19 strain 30/90 was used to construct a gene library in pBluescript II SK(؊) vector in E. coli XL-1-Blue strain. The clones containing recombinant plasmids were screened for the CAMP reaction with Staphylococcus aureus. Those that showed cohemolysis were chosen for further analysis by sequencing. One of these clones, JFRA8, was subcloned to identify the smallest possible DNA fragment containing the CAMP cohemolysin determinant, which was located on a 3,566-bp BamHI-BstXI fragment which specified a 1,026-bp open reading frame. Clones containing recombinant plasmids carrying cam obtained by PCR cloning into E. coli M15 strain secreted an active CAMP cohemolysin. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and Western blot analyses confirmed that the recombinant strain expressed a protein with a molecular mass of 37 kDa and that strains from serotypes 1, 2, 3, 5, 6, and 19 expressed the cohemolysin. The deduced amino acid sequence showed high homology to those of O-sialoglycoprotein endopeptidases. Hydrolysis of radioiodinated glycophorin A confirmed that Cam is a sialoglycoprotease.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

et al. 2002

View full text Add to dashboard Cite

show abstract

“…Sialomucins, including CD164, have the common characteristic of being highly glycosylated polypeptides, containing both O-and N-linked carbohydrate side chains (39,41). Monoclonal antibodies against CD164 that alter the adhesive and proliferative properties of hematopoietic precursors recognize epitopes that are destroyed by treatment of cells with sialidase, which cleaves terminal sialic acid residues on O-or N-linked carbohydrates, or O-sialoglycoprotease, an enzyme that selectively degrades O-sialomucins (9,32). It would be predicted, therefore, that treatment of C2C12 cells with these enzymes would inhibit differentiation.…”

Section: Resultsmentioning

confidence: 99%

“…Treatment of C2C12 cells with O-sialoglycoprotease also inhibited differentiation. This enzyme has a much more restricted set of substrates, apparently recognizing O-linked carbohydrates on mucin domain-containing proteins specifically and cleaving the polypeptide chain nearby (9,32). CD164 may well be a major substrate of O-sialoglycoprotease on C2C12 cells, although the predicted cleavage and release of an aminoterminal fragment do not distinguish between the carbohydrate or peptide sequences lost as being of primary importance.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Role for the Sialomucin CD164 in Myogenic Differentiation by Signal Sequence Trapping in Yeast

Lee

Kang

Krauss

2001

Molecular and Cellular Biology

View full text Add to dashboard Cite

“…1B), indicating that the 9-O-acetyl groups are not carried on the Sias of N-linked oligosaccharides. On the other hand, their staining is markedly reduced by prior treatment of the membrane extract with O-sialoglycoprotease (OSGPase), an enzyme known to selectively proteolyze only mucin-type glycoproteins that carry clustered O-linked oligosaccharides (42,43). To confirm that the protein bands found by SDS-PAGE represent cell surface 9-O-acetylation, intact MEL cells were studied by flow cytometry for staining with the CHE-FcD probe, with and without prior treatment with OSGPase.…”

Section: -O-acetylation Of Sias On Mel Cells Is Predominantly Expresmentioning

confidence: 99%

Regulation of Sialic Acid 9-O-Acetylation during the Growth and Differentiation of Murine Erythroleukemia Cells

Shi

Chammas²,

Varki

1996

Journal of Biological Chemistry

View full text Add to dashboard Cite

Sialic acids are typically found at the terminal position on vertebrate oligosaccharides. They are sometimes modified by an O-acetyl ester at the 9-position, potentially altering recognition of sialic acid by antibodies, lectins, and viruses. 9-O-Acetylation is known to be selectively expressed on gangliosides in melanoma cells and on N-linked chains in hepatocytes. Using a recently developed probe, we show here that in murine erythroleukemia cells, this modification is selectively expressed on another class of oligosaccharides, O-linked chains carried on cell surface sialomucins. These cells also express 9-O-acetylation on the ganglioside G D3 , but this modification appears to be undetectable on the cell surface. Increasing cell density in culture is associated with a decrease in cell surface 9-O-acetylation of sialomucins. This change correlates with the spontaneous differentiation toward a mature erythroid phenotype. This downregulation upon differentiation and entry into the G 0 /G 1 stage of the cell cycle is confirmed by differentiationinducing agents. In contrast, cells arrested in G 2 /M by the microtubule depolymerizing agent nocodazole show increased expression of cell surface 9-O-acetylated sialomucins (but not the 9-O-acetylated ganglioside). However, the microtubule stabilizer taxol does not induce this increase, showing that the nocodazole effect is independent of cell cycle stage. Indeed, direct analysis showed no correlation of 9-O-acetylation with cell cycle stage in rapidly growing cells, and shorter treatments with nocodazole also increased expression. Western blots of cell extracts confirmed that changes caused by differentiation and nocodazole are not due to redistribution of molecules from the cell surface. Indeed, following selective removal of 9-O-acetyl groups from the cell surface by a specific esterase, the recovery of expression is mediated by new synthesis rather than by redistribution from an internal pool. Thus, 9-O-acetylation on these sialomucins appears to be primarily regulated by the rate of synthesis, and the increase with nocodazole treatment is likely due to the inhibition of turnover of cell surface molecules. These data show that 9-O-acetylation of sialic acids in murine erythroleukemia cells is a highly regulated modification, being selectively expressed in a cell type-specific manner on certain classes of oligosaccharides and differentially regulated with regard to subcellular localization and to the state of cellular differentiation.

show abstract

[47] O-sialoglycoprotease from Pasteurella haemolytica

Cited by 40 publications

References 22 publications

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

Identification and Characterization of CAMP Cohemolysin as a Potential Virulence Factor of Riemerella anatipestifer

Identification of a Role for the Sialomucin CD164 in Myogenic Differentiation by Signal Sequence Trapping in Yeast

Regulation of Sialic Acid 9-O-Acetylation during the Growth and Differentiation of Murine Erythroleukemia Cells

Contact Info

Product

Resources

About