Effects of amino acid substitutions outside an antigenic site on protein binding to monoclonal antibodies of predetermined specificity obtained by peptide immunization: Demonstration with region 145?151 (antigenic site 5) of myoglobin

1992 ◽  
Vol 11 (6) ◽  
pp. 687-698 ◽  
Author(s):  
Mohamed-Salah I. Abaza ◽  
M. Zouhair Atassi
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Protein Binding ◽  
Antigenic Site ◽  
Amino Acid Substitutions ◽  
Predetermined Specificity

scholarly journals Characterization of Mouse Monoclonal Antibodies Against the HA of A(H7N9) Influenza Virus

Viruses ◽  
2019 ◽  
Vol 11 (2) ◽  
pp. 149 ◽  
Author(s):  
Mutsumi Ito ◽  
Seiya Yamayoshi ◽  
Kazushi Murakami ◽  
Kenji Saito ◽  
Atsuo Motojima ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Antigenic Site ◽  
Prototype Strain ◽  
Human Infection ◽  
Antigenic Drift ◽  
Amino Acid Substitutions ◽  
H7n9 Virus ◽  
Lethal Infection

Many cases of human infection with the H7N9 virus have been detected in China since 2013. H7N9 viruses are maintained in chickens and are transmitted to humans at live bird markets. During circulation in birds, H7N9 viruses have accumulated amino acid substitutions in their hemagglutinin (HA), which resulted in an antigenically change in the recent H7N9 viruses. Here, we characterized 46 mouse monoclonal antibodies against the HA of the prototype strain. 16 H7-HA-specific monoclonal antibodies (mAbs) possessed hemagglutination inhibition (HI) and neutralization activities by recognizing the major antigenic site A; four other H7-HA-specific clones also showed HI and neutralizing activities via recognition of the major antigenic sites A and D; seven mAbs that reacted with several HA subtypes and possibly recognized the HA stem partially protected mice from lethal infection with prototype H7N9 virus; and the remaining 19 mAbs had neither HI nor neutralization activity. All human H7N9 viruses tested showed a similar neutralization sensitivity to the first group of 16 mAbs, whereas human H7N9 viruses isolated in 2016‒2017 were not neutralized by a second group of 4 mAbs. These results suggest that amino acid substitutions at the epitope of the second mAb group appear to be involved in the antigenic drift of the H7N9 viruses. Further analysis is required to fully understand the antigenic change in H7N9 viruses.

scholarly journals Antigenic and genetic analysis of equine influenza viruses from tropical Africa in 1991

1996 ◽  
Vol 117 (2) ◽  
pp. 367-374 ◽  
Author(s):  
C. A. O. Adeyefa ◽  
M. L. James ◽  
J. W. McCauley
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Antigenic Site ◽  
Glycosylation Site ◽  
Influenza Viruses ◽  
Amino Acid Substitutions ◽  
Antigenic Analysis ◽  
Equine Influenza ◽  
Antigenic Sites ◽  
European Strain

SummaryA detailed analysis of equine (H3N8) influenza viruses isolated in Nigeria during early 1991 has been undertaken. Antigenic analysis and the complete nucleotide sequence of the HA gene of three Nigerian equine influenza viruses A/eq/Ibadan/4/91, A/eq/Ibadan/6/91 and A/eq/Ibadan/9/91 are presented and limited sequence analysis of each of the genes encoding the internal polypeptides of the virus has been carried out. These results establish that, despite the geographical location from which these viruses were isolated, two were similar to the viruses which were concurrently causing disease in Europe in 1989 and 1991 and were related to viruses that have been predominating in horses since 1985. The third was more closely related to viruses isolated from 1991 onward in Europe but also in other parts of the globe. A comparison of the nucleotide sequence of two of the viruses isolated in Nigeria (A/eq/Ibadan/4/91 and A/eq/Ibadan/6/91) with a European strain (A/eq/Suffolk/89) showed limited variation in the haemagglutinin gene which caused amino acid substitutions in one of the antigenic sites: this mutation resulted in the potential production of a new glycosylation site in antigenic site A. The other Nigerian virus (A/eq/Ibadan/9/91) showed only a single one amino acid change from another European strain (A/eq/Arundel/12369/91). The two distinct Nigerian viruses had several amino acid substitutions in the antigenic sites of the haemagglutinin glycoprotein.

scholarly journals Generation of Recombinant Rotavirus with an Antigenic Mosaic of Cross-Reactive Neutralization Epitopes on VP4

2008 ◽  
Vol 82 (13) ◽  
pp. 6753-6757 ◽  
Author(s):  
Satoshi Komoto ◽  
Masanori Kugita ◽  
Jun Sasaki ◽  
Koki Taniguchi
Keyword(s):  
Amino Acids ◽  
Monoclonal Antibodies ◽  
Amino Acid ◽  
Reverse Genetics ◽  
Amino Acid Substitutions ◽  
Neutralization Epitope ◽  
First Report ◽  
P Type

ABSTRACT Recombinant rotavirus (RV) with cDNA-derived chimeric VP4 was generated using recently developed reverse genetics for RV. The rescued virus, KU//rVP4(SA11)-II(DS-1), contains SA11 (simian RV strain, G3P[2])-based VP4, in which a cross-reactive neutralization epitope (amino acids 381 to 401) on VP5* is replaced by the corresponding sequence of a different P-type DS-1 (human RV strain, G2P[4]). Serological analyses with a panel of anti-VP4- and -VP7-neutralizing monoclonal antibodies revealed that the rescued virus carries a novel antigenic mosaic of cross-reactive neutralization epitopes on its VP4 surface. This is the first report of the generation of a recombinant RV with artificial amino acid substitutions.

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