Paramyxovirus fusion (F) protein and hemagglutinin-neuraminidase (HN) protein interactions: intracellular retention of F and HN does not affect transport of the homotypic HN or F protein.
To investigate a possible intracellular coassociation of the paramyxovirus simian virus 5 (SV5) and human parainfluenza virus type 3 (HPIV-3) fusion (F) and hemagglutinin-neuraminidase (HN) glycoproteins in a living cell, without resorting to chemical crosslinking and antibody coimmunoprecipitation, we tagged the cytoplasmic N-terminus of SV5 HN with a RRRRR motif and HPIV-3 HN with a RRR motif for endoplasmic reticulum (ER) retention. In addition, we tagged the cytoplasmic C-terminus of SV5 and HPIV-3 F with a KK motif. The RRR- or RRRRR-tagged HN molecules were coexpressed in mammalian cells together with the homologous wt F proteins, and the KK-tagged F molecules were coexpressed with the homologous wt HN proteins, and in each case the transport of the wt F or HN molecules was investigated. The data suggest that an association of F and HN of sufficient affinity to alter the transport of the reporter molecule does not occur intracellularly in the ER or the Golgi apparatus.
Paterson
R G
RG
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208-3500, USA.
Johnson
M L
ML
Lamb
R A
RA
D001692:Biological Transport; D015707:HN Protein / Q000235:genetics / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D010224:Parainfluenza Virus 3, Human / Q000378:metabolism*; D011485:Protein Binding; D018108:Respirovirus / Q000378:metabolism*; D014162:Transfection; D014760:Viral Fusion Proteins / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism
D015707:HN Protein; D014760:Viral Fusion Proteins; D014764:Viral Proteins