Objectives: This work focuses on human cytomegalovirus (HCMV) UL73, which encodes for a putative transmembrane glycoprotein that is highly conserved among herpesviruses. Study Design: pUL73 expression was analyzed both in transiently transfected and in HCMV-infected cells using a pUL73-specific antiserum by immunoblot and immunofluorescence. Sequencing analysis from several clinical isolates and laboratory-adapted strains was also performed. Results: pUL73 expressed in transiently transfected cells consists in a polypeptide of the expected size (15-18 kd) with cytoplasmic localization. In infected cells, pUL73 is expressed with true-late kinetics and localizes both in perinuclear granular formations and on the cell surface. A broad band (39-53 kd), sensitive to O-glycosidase digestion was detected in purified virus. In addition, sequence analysis showed that the N-terminal portion of pUL73 from clinical isolates is highly polymorphic. Conclusions: UL73 encodes for a new structural glycoprotein (gpUL73) expressed on the cell surface of infected cells and highly polymorphic among clinical isolates.
Dal Monte P., Pignatelli S., Mach M., Landini M.P. (2001). The product of human cytomegalovirus UL73 is a new polymorphic structural glycoprotein (gpUL73). JOURNAL OF HUMAN VIROLOGY, 4(1), 26-34.
The product of human cytomegalovirus UL73 is a new polymorphic structural glycoprotein (gpUL73)
Dal Monte P.;Pignatelli S.;Landini M. P.
2001
Abstract
Objectives: This work focuses on human cytomegalovirus (HCMV) UL73, which encodes for a putative transmembrane glycoprotein that is highly conserved among herpesviruses. Study Design: pUL73 expression was analyzed both in transiently transfected and in HCMV-infected cells using a pUL73-specific antiserum by immunoblot and immunofluorescence. Sequencing analysis from several clinical isolates and laboratory-adapted strains was also performed. Results: pUL73 expressed in transiently transfected cells consists in a polypeptide of the expected size (15-18 kd) with cytoplasmic localization. In infected cells, pUL73 is expressed with true-late kinetics and localizes both in perinuclear granular formations and on the cell surface. A broad band (39-53 kd), sensitive to O-glycosidase digestion was detected in purified virus. In addition, sequence analysis showed that the N-terminal portion of pUL73 from clinical isolates is highly polymorphic. Conclusions: UL73 encodes for a new structural glycoprotein (gpUL73) expressed on the cell surface of infected cells and highly polymorphic among clinical isolates.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
