Single Amino Acid Codon Changes Detected in Louping Ill Virus Antibody-Resistant Mutants with Reduced Neurovirulence

1993 ◽  
Vol 74 (5) ◽  
pp. 931-935 ◽  
Author(s):  
W. R. Jiang ◽  
A. Lowe ◽  
S. Higgs ◽  
H. Reid ◽  
E. A. Gould
Keyword(s):  
Amino Acid ◽  
Single Amino Acid ◽  
Virus Antibody ◽  
Louping Ill ◽  
Resistant Mutants ◽  
Amino Acid Codon

scholarly journals Characterization of a Natural Mutation in an Antigenic Site on the Fusion Protein of Measles Virus That Is Involved in Neutralization

1999 ◽  
Vol 73 (1) ◽  
pp. 787-790 ◽  
Author(s):  
Joël Fayolle ◽  
Bernard Verrier ◽  
Robin Buckland ◽  
T. Fabian Wild
Keyword(s):  
Amino Acid ◽  
Virus Strain ◽  
Measles Virus ◽  
Antigenic Site ◽  
Single Amino Acid ◽  
Nucleotide Sequence Analysis ◽  
Single Amino Acid Change ◽  
Resistant Mutants ◽  
Natural Mutation

ABSTRACT Although measles virus is an antigenically monotypic virus, nucleotide sequence analysis of the hemagglutinin and nucleoprotein genes has permitted the differentiation of a number of genotypes. In contrast, the fusion (F) protein is highly conserved; only three amino acid changes have been reported over a 40-year period. We have isolated a measles virus strain which did not react with an anti-F monoclonal antibody (MAb) which we had previously shown to be directed against a dominant antigenic site. This virus strain, Lys-1, had seven amino acid changes compared with the Edmonston strain. We have shown that a single amino acid at position 73 is responsible for its nonreactivity with the anti-F MAb. With the same MAb, antibody-resistant mutants were prepared from the vaccine strain. A single amino acid change at position 73 (R→W) was observed. The possibility of selecting measles virus variants in vaccinated populations is discussed.

Single Amino Acid Based Self-Assemblies of Cysteine and Methionine

2018 ◽  
Author(s):  
Nidhi Gour ◽  
Bharti Koshti ◽  
Chandra Kanth P. ◽  
Dhruvi Shah ◽  
Vivek Shinh Kshatriya ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Self Assembly ◽  
Aromatic Amino Acids ◽  
Neutral Condition ◽  
Single Amino Acid ◽  
Binding Assays ◽  
Human Neuroblastoma ◽  
Cytotoxicity Assays ◽  
First Time

We report for the very first time self-assembly of Cysteine and Methionine to discrenible strucutres under neutral condition. To get insights into the structure formation, thioflavin T and Congo red binding assays were done which revealed that aggregates may not have amyloid like characteristics. The nature of interactions which lead to such self-assemblies was purported by coincubating assemblies in urea and mercaptoethanol. Further interaction of aggregates with short amyloidogenic dipeptide diphenylalanine (FF) was assessed. While cysteine aggregates completely disrupted FF fibres, methionine albeit triggered fibrillation. The cytotoxicity assays of cysteine and methionine structures were performed on Human Neuroblastoma IMR-32 cells which suggested that aggregates are not cytotoxic in nature and thus, may not have amyloid like etiology. The results presented in the manuscript are striking, since to the best of our knowledge,this is the first report which demonstrates that even non-aromatic amino acids (cysteine and methionine) can undergo spontaneous self-assembly to form ordered aggregates.

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