PubMed:2157800 JSONTXT

{"project":"LitCoin-PubTator-for-Tuning","denotations":[{"id":"1","span":{"begin":49,"end":70},"obj":"OrganismTaxon"},{"id":"10","span":{"begin":189,"end":210},"obj":"OrganismTaxon"},{"id":"11","span":{"begin":212,"end":216},"obj":"OrganismTaxon"},{"id":"12","span":{"begin":423,"end":448},"obj":"ChemicalEntity"},{"id":"13","span":{"begin":454,"end":469},"obj":"ChemicalEntity"},{"id":"14","span":{"begin":780,"end":789},"obj":"OrganismTaxon"},{"id":"15","span":{"begin":935,"end":939},"obj":"OrganismTaxon"},{"id":"16","span":{"begin":947,"end":952},"obj":"OrganismTaxon"},{"id":"17","span":{"begin":1039,"end":1043},"obj":"OrganismTaxon"}],"attributes":[{"id":"A15","pred":"tao:has_database_id","subj":"15","obj":"Tax:10359"},{"id":"A16","pred":"tao:has_database_id","subj":"16","obj":"Tax:9606"},{"id":"A10","pred":"tao:has_database_id","subj":"10","obj":"Tax:10359"},{"id":"A14","pred":"tao:has_database_id","subj":"14","obj":"Tax:9606"},{"id":"A11","pred":"tao:has_database_id","subj":"11","obj":"Tax:10359"},{"id":"A1","pred":"tao:has_database_id","subj":"1","obj":"Tax:10359"},{"id":"A13","pred":"tao:has_database_id","subj":"13","obj":"MESH:D009844"},{"id":"A17","pred":"tao:has_database_id","subj":"17","obj":"Tax:10359"}],"text":"Structural and immunological characterization of human cytomegalovirus gp55-116 (gB) expressed in insect cells.\nThe gene encoding the major envelope glycoprotein complex, gp55-116 (gB), of human cytomegalovirus (HCMV) was expressed at high levels in insect cells utilizing a recombinant baculovirus. The mature intracellular form of the insect-derived gp55-116 was a protein of Mr 150K which contained approximately 50K of N-linked oligosaccharides. The oligosaccharide linkages were almost exclusively endoglycosidase H-sensitive. The 150K protein was processed, presumably by proteolytic cleavage, to yield at least one of the previously defined cleavage products of the gp55-116. This processing step was significantly less efficient in insect cells than the analogous step in mammalian cells. Finally, the insect-derived gp55-116 was highly immunogenic in experimental animals and readily recognized by antibodies contained within HCMV-immune human serum, suggesting that this recombinant protein warrants further study as a potential HCMV subunit vaccine candidate."}

{"project":"LitCoin-PubTator-for-Tuning-SeqVar","denotations":[{"id":"T1","span":{"begin":381,"end":385},"obj":"SequenceVariant"},{"id":"T2","span":{"begin":416,"end":419},"obj":"SequenceVariant"},{"id":"T3","span":{"begin":536,"end":540},"obj":"SequenceVariant"}],"text":"Structural and immunological characterization of human cytomegalovirus gp55-116 (gB) expressed in insect cells.\nThe gene encoding the major envelope glycoprotein complex, gp55-116 (gB), of human cytomegalovirus (HCMV) was expressed at high levels in insect cells utilizing a recombinant baculovirus. The mature intracellular form of the insect-derived gp55-116 was a protein of Mr 150K which contained approximately 50K of N-linked oligosaccharides. The oligosaccharide linkages were almost exclusively endoglycosidase H-sensitive. The 150K protein was processed, presumably by proteolytic cleavage, to yield at least one of the previously defined cleavage products of the gp55-116. This processing step was significantly less efficient in insect cells than the analogous step in mammalian cells. Finally, the insect-derived gp55-116 was highly immunogenic in experimental animals and readily recognized by antibodies contained within HCMV-immune human serum, suggesting that this recombinant protein warrants further study as a potential HCMV subunit vaccine candidate."}