Adsorption of LLCMK2 cell-grown Sendai virus onto human red blood cells and its release from the virus adsorbed cells.
An early stage of virus adsorption was studied in a system of Sendai virus metabolically labeled with [3H]leucine in LLCMK2 cells and of human red blood cells (RBCs). The efficiency of viral release from the virus-bound RBCs by incubation at 37 C depended on the number of virus particles which had been used for adsorption onto the RBC at 4 C. When 7.8 x 10(2) virus particles were previously adsorbed onto the RBC at 4 C, most of the viruses were dissociated from the RBC at 37 C. In the case of adsorption of 3 to 12 virus particles per RBC, however, most of the viruses were not dissociated from the RBC by incubation at 37 C. Such RBC-bound viruses were released by incubation with various bacterial neuraminidases (Clostridium perfringens, etc.) or with a large number of LLCMK2 cell-grown Sendai virus (LLCMK2-Sendai) particles, but not released by treatment with hemagglutinin-neuraminidase protein (Sendai-gp) isolated from egg-grown Sendai virus.
Komatsu
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Department of Immunology, School of Hygienic Sciences, Kitasato University, Kanagawa.
Tozawa
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D000327:Adsorption; D004912:Erythrocytes / Q000382:microbiology*; D015707:HN Protein; D006801:Humans; D066298:In Vitro Techniques; D009439:Neuraminidase / Q000494:pharmacology; D010222:Parainfluenza Virus 1, Human / Q000502:physiology*; D011991:Receptors, Virus / Q000187:drug effects / Q000502:physiology*; D014759:Viral Envelope Proteins / Q000502:physiology; D014760:Viral Fusion Proteins / Q000502:physiology; D014776:Virus Cultivation
D015707:HN Protein; D011991:Receptors, Virus; D014759:Viral Envelope Proteins; D014760:Viral Fusion Proteins; D009439:Neuraminidase