Complex formation between the spike protein and the membrane protein during mouse hepatitis virus assembly.
Using different approaches we have demonstrated the formation of a complex between the S protein and the M protein in the process of mouse hepatitis virus (MHV) assembly. Preservation of the M/S heterocomplexes was critically dependent on the solubilization conditions. Pulse-chase labeling of MHV-infected cells followed by a co-immunoprecipitation assay revealed that newly synthesized S and M engage in complex formation with different kinetics, the S protein reacting much slower. Sedimentation experiments showed the M/S heteromultimer complexes to be very large. A model for the role of the complex formation in MHV assembly is presented.
Opstelten
D J
DJ
Department of Infectious Diseases and Immunology, Faculty of Veterinary Medicine, University of Utrecht, The Netherlands.
Horzinek
M C
MC
Rottier
P J
PJ
D000818:Animals; D002460:Cell Line; D000086862:Coronavirus M Proteins; D008562:Membrane Glycoproteins / Q000378:metabolism*; D009024:Morphogenesis; D006517:Murine hepatitis virus / Q000378:metabolism* / Q000648:ultrastructure; D011485:Protein Binding; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins / Q000378:metabolism*; D014763:Viral Matrix Proteins / Q000378:metabolism*; D014771:Virion / Q000378:metabolism*
D000086862:Coronavirus M Proteins; D008562:Membrane Glycoproteins; D064370:Spike Glycoprotein, Coronavirus; D014759:Viral Envelope Proteins; D014763:Viral Matrix Proteins; C578557:spike glycoprotein, SARS-CoV; C578553:spike protein, mouse hepatitis virus