Comparison of receptor-binding properties among influenza C virus isolates
Autor: | Yasushi Muraki, Masami Matsuzaki, Yoko Matsuzaki, Fumio Kitame, Seiji Hongo, Kiyoto Nakamura, Kanetsu Sugawara |
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Rok vydání: | 1995 |
Předmět: |
Cancer Research
Erythrocytes Influenzavirus C Hemagglutinins Viral Biology Receptor binding site Mice Structure-Activity Relationship Viral Proteins Virology Animals Humans Amino Acids Peptide sequence Glycoproteins chemistry.chemical_classification Hemagglutinin esterase Hemagglutination Molecular biology Amino acid Agglutination (biology) Titer Infectious Diseases chemistry Receptors Virus Influenza C Virus Chickens Viral Fusion Proteins |
Zdroj: | Virus Research. 38:291-296 |
ISSN: | 0168-1702 |
Popis: | A total of 10 influenza C virus strains isolated recently in Yamagata City, Japan and shown to belong to the same lineage was compared for the ability to agglutinate chicken and mouse erythrocytes under various conditions. C/Yamagata/10/89 was unique in lacking the ability to agglutinate chicken erythrocytes at a temperatureor = 4 degrees C. This isolate also agglutinated native mouse erythrocytes only very inefficiently, although the high agglutination titer was obtained with the glutaraldehyde-fixed cells. Furthermore, it was found that C/Yamagata/4/88, unlike the other isolates, agglutinated erythrocytes from chickens to lower titers than those from mice, even when assayed at 0 degree C. Comparison of the deduced amino acid sequence of hemagglutinin-esterase among the 6 representative strains including two older isolates, C/Yamagata/26/81 and C/Nara/2/85, suggested that the failures of C/Yamagata/10/89 to agglutinate chicken erythrocytes ator = 4 degrees C and unfixed mouse erythrocytes to high titers may be due to amino acid changes at residues 337 (Glu--Lys) and 340 (Thr--Tyr), respectively, and that a change at residue 347 (Leu--Ser) may be responsible for the decreased ability of C/Yamagata/4/88 to agglutinate chicken erythrocytes. |
Databáze: | OpenAIRE |
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