Mutation can alter the structure of viral proteins to form different structure. Carbon distribution is responsible for these changes in structure. The carbon distribution in proteins of human Influenza A virus is anal...Mutation can alter the structure of viral proteins to form different structure. Carbon distribution is responsible for these changes in structure. The carbon distribution in proteins of human Influenza A virus is analyzed here. Results reveal that the carbon contents are high in surface proteins, optimum in polymerase proteins and less in nuclear proteins. Polymerase proteins have better carbon distribution pattern than the other proteins. Thymine distribution in different frames of mRNAs are checked as it has link with carbon distribution pattern in the corresponding proteins. Results show that frame 4 is violating from thymine distribution. This is responsible for production of protein with different carbon distribution. Unusual thymine distribution in frame 3 are observed. The thymine distributions are different in viral mRNA compared to normal one. Minimizing the excess thymine in H1N1 mRNAs might improve the protein performance. Mutational study based on carbon distribution should be better exploited for further improving the protein stability, activity and ultimately for gene therapy.展开更多
With the support by the National Natural Science Foundation of China,the research team led by Prof.Yu Hongjie(余宏杰)at the School of Public Health,Fudan University,Key Laboratory of Public Health Safety,Ministry of E...With the support by the National Natural Science Foundation of China,the research team led by Prof.Yu Hongjie(余宏杰)at the School of Public Health,Fudan University,Key Laboratory of Public Health Safety,Ministry of Education,and the Key Laboratory of Surveillance and Early Warning on Infectious Disease,Chinese Center for Disease Control and Prevention,has published the paper entitled“Global epi-展开更多
Antigenic drift forces us to frequently update influenza vaccines; however, the genetic basis for antigenic variation remains largely unknown. In this study, we used clade 7.2 H5 viruses as models to explore the molec...Antigenic drift forces us to frequently update influenza vaccines; however, the genetic basis for antigenic variation remains largely unknown. In this study, we used clade 7.2 H5 viruses as models to explore the molecular determinants of influenza virus antigenic variation. We generated eight monoclonal antibodies(MAbs) targeted to the hemagglutinin(HA) protein of the index virus A/chicken/Shanxi/2/2006 and found that two representative antigenically drifted clade 7.2 viruses did not react with six of the eight MAbs. The E131 N mutation and insertion of leucine at position 134 in the HA protein of the antigenically drifted strains eliminated the reactivity of the virus with the MAbs. We also found that the amino acid N131 in the H5 HA protein is glycosylated. Our results provide experimental evidence that glycosylation and an amino acid insertion or deletion in HA influence antigenic variation.展开更多
文摘Mutation can alter the structure of viral proteins to form different structure. Carbon distribution is responsible for these changes in structure. The carbon distribution in proteins of human Influenza A virus is analyzed here. Results reveal that the carbon contents are high in surface proteins, optimum in polymerase proteins and less in nuclear proteins. Polymerase proteins have better carbon distribution pattern than the other proteins. Thymine distribution in different frames of mRNAs are checked as it has link with carbon distribution pattern in the corresponding proteins. Results show that frame 4 is violating from thymine distribution. This is responsible for production of protein with different carbon distribution. Unusual thymine distribution in frame 3 are observed. The thymine distributions are different in viral mRNA compared to normal one. Minimizing the excess thymine in H1N1 mRNAs might improve the protein performance. Mutational study based on carbon distribution should be better exploited for further improving the protein stability, activity and ultimately for gene therapy.
文摘With the support by the National Natural Science Foundation of China,the research team led by Prof.Yu Hongjie(余宏杰)at the School of Public Health,Fudan University,Key Laboratory of Public Health Safety,Ministry of Education,and the Key Laboratory of Surveillance and Early Warning on Infectious Disease,Chinese Center for Disease Control and Prevention,has published the paper entitled“Global epi-
基金supported by the National Natural Science Foundation of China (31521005, 31672593)the National Key R&D Program of China (2016YFD0500201, 2016YFD0500203)the China Agriculture Research System (CARS-41-G12)
文摘Antigenic drift forces us to frequently update influenza vaccines; however, the genetic basis for antigenic variation remains largely unknown. In this study, we used clade 7.2 H5 viruses as models to explore the molecular determinants of influenza virus antigenic variation. We generated eight monoclonal antibodies(MAbs) targeted to the hemagglutinin(HA) protein of the index virus A/chicken/Shanxi/2/2006 and found that two representative antigenically drifted clade 7.2 viruses did not react with six of the eight MAbs. The E131 N mutation and insertion of leucine at position 134 in the HA protein of the antigenically drifted strains eliminated the reactivity of the virus with the MAbs. We also found that the amino acid N131 in the H5 HA protein is glycosylated. Our results provide experimental evidence that glycosylation and an amino acid insertion or deletion in HA influence antigenic variation.
