Increased binding activity of measles virus to monkey red blood cells after long-term passage in Vero cell cultures

• Published in: Journal of general virology Vol. 75; no. 12; pp. 3511 - 3516
• Main Authors: Shibahara, Katsuki, Hotta, Hak, Katayama, Yuko, Homma, Morio
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01.12.1994
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Cell Membrane - metabolism; Cercopithecus aethiops; Erythrocytes - metabolism; Erythrocytes - physiology; Genetic Variation - genetics; Hemagglutination, Viral - physiology; Hemagglutinins, Viral - biosynthesis; Hemagglutinins, Viral - genetics; Hemagglutinins, Viral - metabolism; Humans; measles virus; Measles virus - growth & development; Measles virus - metabolism; Molecular Sequence Data; Serial Passage; Vero Cells - virology; Viral Plaque Assay; Viral Proteins - metabolism
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-75-12-3511

Department of Microbiology, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe, Hyogo 650, Japan Recent field isolates of measles virus (MV) obtained by using B95-8 cells have been reported not to agglutinate African green monkey red blood cells (AGM-RBC). Vero cell-adapted, plaque-forming strains derived from three field isolates at the third passage in Vero cell cultures (T8Ve-3, T11Ve-3 and N13Ve-3) also exhibited markedly decreased binding activity, as determined by infectivity-absorption and haemadsorption tests. On the other hand, binding activity of the respective strains at the twentieth passage (T8Ve-20, T11Ve-20 and N13Ve-20) increased to practically the same level as that of the Edmonston strain, a standard strain of MV passaged long-term. A membrane immunofluorescence test revealed that the decreased binding activity to AGM-RBC of T8Ve-3, T11Ve-3 and N13Ve-3 was not due to decreased expression of the haemagglutinin (H) protein on the cell surface. The deduced amino acid sequence of the H protein synthesized in T11Ve-3-infected cells was identical to that in T11Ve-20-infected cells, although a single amino acid alteration was observed when T8Ve-3 was compared with T8Ve-20. Similarly, approximately half of the N13Ve-20-infected cells synthesized an H protein identical to that produced in N13Ve-3-infected cells, and nevertheless, exhibited markedly increased haemadsorption. The present results suggest that a viral protein(s) other than the H protein contributed to the binding activity of MV to AGM-RBC. Received 19 April 1994; accepted 2 August 1994.