scholarly journals Analysis of Amino Acid Mutations of the Foot-and-Mouth Disease Virus Serotype O Using both Heparan Sulfate and JMJD6 Receptors

Viruses ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 1012 ◽  
Author(s):  
Gyeongmin Lee ◽  
Ji-Hyeon Hwang ◽  
Aro Kim ◽  
Jong-Hyeon Park ◽  
Min Ja Lee ◽  
...  
Keyword(s):  
Amino Acid ◽  
Heparan Sulfate ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Amino Acid Sequences ◽  
Cell Adaptation ◽  
Field Virus ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Foot And Mouth

Foot-and-mouth disease (FMD) is an economically devastating animal disease. Adapting the field virus to cells is critical to the vaccine production of FMD viruses (FMDV), and heparan sulfate (HS) and Jumonji C-domain-containing protein 6 (JMJD6) are alternative receptors of cell-adapted FMDV. We performed serial passages of FMDV O/SKR/Andong/2010, classified as the O/Mya-98 topotype/lineage and known as a highly virulent strain, to develop a vaccine seed virus. We traced changes in the amino acid sequences of the P1 region, plaque phenotypes, and the receptor usage of the viruses, and then structurally analyzed the mutations. VP3 H56R and D60G mutations were observed in viruses using the HS receptor and led to changes in the hydrogen bonding between VP3 56 and 60. A VP1 P208L mutation was observed in the virus using the JMJD6 receptor during cell adaptation, enabling the interaction with JMJD6 through the formation of a new hydrogen bond with JMJD6 residue 300. Furthermore, VP1 208 was near the VP1 95/96 amino acids, previously reported as critical mutations for JMJD6 receptor interactions. Thus, the mutation at VP1 208 could be critical for cell adaptation related to the JMJD6 receptor and may serve as a basis for mechanism studies on FMDV cell adaptation.

scholarly journals Antigenic variation of foot-and-mouth disease virus serotype A

2014 ◽  
Vol 95 (2) ◽  
pp. 384-392 ◽  
Author(s):  
A. B. Ludi ◽  
D. L. Horton ◽  
Y. Li ◽  
M. Mahapatra ◽  
D. P. King ◽  
...  
Keyword(s):  
Vaccine Strain ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Serotype A ◽  
Field Virus ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Foot And Mouth ◽  
Potential Vaccine ◽  
Antigenic Relationships

The current measures to control foot-and-mouth disease (FMD) include vaccination, movement control and slaughter of infected or susceptible animals. One of the difficulties in controlling FMD by vaccination arises due to the substantial diversity found among the seven serotypes of FMD virus (FMDV) and the strains within these serotypes. Therefore, vaccination using a single vaccine strain may not fully cross-protect against all strains within that serotype, and therefore selection of appropriate vaccines requires serological comparison of the field virus and potential vaccine viruses using relationship coefficients (r 1 values). Limitations of this approach are that antigenic relationships among field viruses are not addressed, as comparisons are only with potential vaccine virus. Furthermore, inherent variation among vaccine sera may impair reproducibility of one-way relationship scores. Here, we used antigenic cartography to quantify and visualize the antigenic relationships among FMD serotype A viruses, aiming to improve the understanding of FMDV antigenic evolution and the scope and reliability of vaccine matching. Our results suggest that predicting antigenic difference using genetic sequence alone or by geographical location is not currently reliable. We found co-circulating lineages in one region that were genetically similar but antigenically distinct. Nevertheless, by comparing antigenic distances measured from the antigenic maps with the full capsid (P1) sequence, we identified a specific amino acid substitution associated with an antigenic mismatch among field viruses and a commonly used prototype vaccine strain, A22/IRQ/24/64.

Antiviral potential of ivermectin against foot-and-mouth disease virus, serotype O, A and Asia-1

2021 ◽  
pp. 104914
Author(s):  
Zahra Naeem ◽  
Sohail Raza ◽  
Saba Afzal ◽  
Ali Ahmad Sheikh ◽  
Muhammad Muddassir Ali ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Serotype O ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Foot And Mouth

scholarly journals Novel antibody binding determinants on the capsid surface of serotype O foot-and-mouth disease virus

2014 ◽  
Vol 95 (5) ◽  
pp. 1104-1116 ◽  
Author(s):  
Amin S. Asfor ◽  
Sasmita Upadhyaya ◽  
Nick J. Knowles ◽  
Donald P. King ◽  
David J. Paton ◽  
...  
Keyword(s):  
Amino Acid ◽  
Guinea Pig ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Amino Acid Residues ◽  
Serotype O ◽  
Antigenic Sites ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
The Impact

Five neutralizing antigenic sites have been described for serotype O foot-and-mouth disease viruses (FMDV) based on monoclonal antibody (mAb) escape mutant studies. However, a mutant virus selected to escape neutralization of mAb binding at all five sites was previously shown to confer complete cross-protection with the parental virus in guinea pig challenge studies, suggesting that amino acid residues outside the mAb binding sites contribute to antibody-mediated in vivo neutralization of FMDV. Comparison of the ability of bovine antisera to neutralize a panel of serotype O FMDV identified three novel putative sites at VP2-74, VP2-191 and VP3-85, where amino acid substitutions correlated with changes in sero-reactivity. The impact of these positions was tested using site-directed mutagenesis to effect substitutions at critical amino acid residues within an infectious copy of FMDV O1 Kaufbeuren (O1K). Recovered viruses containing additional mutations at VP2-74 and VP2-191 exhibited greater resistance to neutralization with both O1K guinea pig and O BFS bovine antisera than a virus that was engineered to include only mutations at the five known antigenic sites. The changes at VP2-74 and VP3-85 are adjacent to critical amino acids that define antigenic sites 2 and 4, respectively. However VP2-191 (17 Å away from VP2-72), located at the threefold axis and more distant from previously identified antigenic sites, exhibited the most profound effect. These findings extend our knowledge of the surface features of the FMDV capsid known to elicit neutralizing antibodies, and will improve our strategies for vaccine strain selection and rational vaccine design.

A recombinant protein-based ELISA for detecting antibodies to foot-and-mouth disease virus serotype Asia 1

2009 ◽  
Vol 159 (1) ◽  
pp. 112-118 ◽  
Author(s):  
Young-Joon Ko ◽  
Hye-Young Jeoung ◽  
Hyang-Sim Lee ◽  
Byung-Sik Chang ◽  
Seung-Min Hong ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Foot And Mouth ◽  
Serotype Asia 1
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