Evidence for conformational changes in elongation factor Tu induced by GTP and GDP.
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Biomedical subjects
Publications and source records attributed to D L Miller.
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A prospective serological and clinical study of the epidemics due to the A2/Hong Kong/68 influenza virus was made during the winters 1968-9 and 1969-70 in volunteer subjects in the Royal Air Force. In October 1968 nearly all subjects had haemagglutination inhibiting (HI) antibody to the A2/Singapore/57 virus and more than half had antibody to strains more recently prevalent in Britain. The proportion with HI antibody to A2/Hong Kong/68 increased from 31% in October 1968 (most at low titres) to 44% after the first epidemic and 72% after the second (most at high titres). Serological infection rates were much lower in those who had detectable antibody at the beginning of each winter than in those who did not. Respiratory illnesses coupled with serological evidence of influenza infection during the winter were rare in persons with an initial titre of HI antibody of 1/40 or more. Infection in the first winter conferred complete protection against infection, with or without illness, in the second. In both epidemics about half those with serological evidence of infection had no reported illness.
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An illness consisting of vomiting, fever, and mild diarrhoea after a short incubation period was observed in a boarding school and reproduced in volunteers who received filtered extracts of faeces from a typical case. The main discriminatory diagnostic feature of the illness in volunteers was vomiting. The faeces contained no pathogenic bacteria nor any virus that could be detected in tissue cultures and there was no evidence that an infective agent could be grown in organ cultures of human intestine. The agent was shown to be ether stable and passed a 50-nm filter. Laboratory studies on another agent of uncertain significance and obtained in other epidemics are briefly described.
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The binding of elongation factor EF G to ribosomes inhibits the subsequent reaction of the ribosomes with the ternary complex aminoacyl-tRNA.EF Tu.GTP. Both the hydrolysis of GTP and the binding of aminoacyl-tRNA to ribosomes are nearly abolished by the previous binding of factor EF G to ribosomes in the presence of either fusidic acid plus either GTP or a nonhydrolyzable analog of GTP. The results suggest that each elongation factor binds to the same region on the ribosome. The GTPase activities of both factors EF G and EF Tu may be activated by interaction at the same ribosomal site, as has been previously suggested by others.
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