Immunoelectron Microscopy of Parainfluenza Virion Glycoproteins with Polyclonal and Monoclonal Antibodies: Movement of Glycoprotein with Monoclonal Antibody
F Hernández, Patrícia Rivera, Hideki Tozawa, Y Hosaka
Abstract
F Hernández, Patrícia Rivera, Hideki Tozawa, Y Hosaka
Abstract
Two glycoproteins (HN and F) of parainfluenza virus were immunogold-labeled with polyclonal and monoclonal antibodies, respectively, and their labeling patterns were compared. Both glycoproteins HN and F were efficiently and homogeneously labeled with polyclonal antibodies, whereas they were labeled much less and heterogeneously with monoclonal antibodies. When either protein was initially labeled with monoclonal antibody, and then the other one, with polyclonal antibody, immunolabels of two glycoproteins were almost completely segregated. Although this segregation deformed virion morphology, it supported the concept of monoclonal antibody-mediated movements of glycoproteins.
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Two glycoproteins (HN and F) of parainfluenza virus were immunogold-labeled with polyclonal and monoclonal antibodies, respectively, and their labeling patterns were compared. Both glycoproteins HN and F were efficiently and homogeneously labeled with polyclonal antibodies, whereas they were labeled much less and heterogeneously with monoclonal antibodies. When either protein was initially labeled with monoclonal antibody, and then the other one, with polyclonal antibody, immunolabels of two glycoproteins were almost completely segregated. Although this segregation deformed virion morphology, it supported the concept of monoclonal antibody-mediated movements of glycoproteins.
Key concepts: Polyclonal antibodies, Monoclonal antibody, Glycoprotein, Immunoelectron microscopy, Antibody, Immunogold labelling, Molecular biology, Monoclonal