SINGLE AMINO-ACID CODON CHANGES DETECTED IN LOUPING ILL VIRUS ANTIBODY-RESISTANT MUTANTS WITH REDUCED NEUROVIRULENCE

被引:95
作者
JIANG, WR
LOWE, A
HIGGS, S
REID, H
GOULD, EA
机构
[1] NERC,INST VIROL & ENVIRONM MICROBIOL,MANSFIELD RD,OXFORD OX1 3SR,ENGLAND
[2] MOREDUN RES INST,EDINBURGH EH17 7JH,MIDLOTHIAN,SCOTLAND
关键词
D O I
10.1099/0022-1317-74-5-931
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Seven mutant viruses were derived from a Scottish strain of louping ill virus using a virus envelope-specific neutralizing monoclonal antibody. None of the mutants was neutralized and immunofluorescence microscopy confirmed that they did not bind to this antibody. Four mutants showed reduced mouse neurovirulence compared with parent virus and two mutants failed to induce protective immune responses in mice challenged with virulent tick-borne encephalitis virus. The mutants with the lowest virulence showed poor or undetectable haemagglutinating activity. The nucleotide sequence of the envelope glycoprotein gene of each of the seven mutants was determined and the deduced amino acid sequence was compared with parent virus. For each mutant, only a single amino acid codon change was detected and all the amino acid substitutions occurred within amino acid positions 308 to 311. A change from the amino acid aspartate to asparagine at amino acid position 308, which represented a potential glycosylation site, was the most effective substitution in reducing mouse neurovirulence. The results demonstrate the importance of critical sites within the envelope glycoprotein as determinants of virus virulence.
引用
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页码:931 / 935
页数:5
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