Crystallization and preliminary x-ray diffraction studies of a monoclonal antibody fab fragment against foot-and-mouth disease virus and of its complex with the main antigenic site peptide

1994 ◽  
Vol 18 (2) ◽  
pp. 201-203 ◽  
Author(s):  
Nuria Verdaguer ◽  
Mauricio G. Mateu ◽  
Jerónimo Bravo ◽  
José Tormo ◽  
Ernest Giralt ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Disease Virus ◽  
Antigenic Site ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
X Ray Diffraction ◽  
Fab Fragment ◽  
X Ray ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Crystallization and preliminary X-ray diffraction analysis of foot-and-mouth disease virus

1987 ◽  
Vol 196 (3) ◽  
pp. 591-597 ◽  
Author(s):  
Graham Fox ◽  
David Stuart ◽  
K.Ravindra Acharya ◽  
Elizabeth Fry ◽  
David Rowlands ◽  
...  
Keyword(s):  
Diffraction Analysis ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
X Ray Diffraction ◽  
X Ray ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Crystallization and preliminary X-ray diffraction studies of the Lb proteinase from foot-and-mouth disease virus

1996 ◽  
Vol 5 (9) ◽  
pp. 1931-1933 ◽  
Author(s):  
Alba Guarnéa ◽  
Núaria Verdaguer ◽  
Ignasi Fita ◽  
Regina Kirchweger ◽  
Hans-Dieter Liebig ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
X Ray Diffraction ◽  
X Ray ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Identification of a conserved linear neutralizing epitope recognized by monoclonal antibody 9A9 against serotype A foot-and-mouth disease virus

2016 ◽  
Vol 161 (10) ◽  
pp. 2705-2716 ◽  
Author(s):  
Weifeng Liang ◽  
Guohui Zhou ◽  
Wenming Liu ◽  
Baolin Yang ◽  
Chaosi Li ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Neutralizing Epitope ◽  
Serotype A ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals (F)uridylylated Peptides Linked to VPg1 of Foot-and- Mouth Disease Virus (FMDV): Design, Synthesis and X-Ray Crystallography of the Complexes with FMDV RNA-Dependent RNA Polymerase

Molecules ◽  
2019 ◽  
Vol 24 (13) ◽  
pp. 2360 ◽  
Author(s):  
Sonia de Castro ◽  
Cristina Ferrer-Orta ◽  
Alberto Mills ◽  
Gloria Fernández-Cureses ◽  
Federico Gago ◽  
...  
Keyword(s):  
Rna Polymerase ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Viral Rna ◽  
Hydroxyl Group ◽  
Rna Dependent Rna Polymerase ◽  
X Ray ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Foot-and-mouth disease virus (FMDV) is an RNA virus belonging to the Picornaviridae family that contains three small viral proteins (VPgs), named VPg1, VPg2 and VPg3, linked to the 5′-end of the viral genome. These VPg proteins act as primers for RNA replication, which is initiated by the consecutive binding of two UMP molecules to the hydroxyl group of Tyr3 in VPg. This process, termed uridylylation, is catalyzed by the viral RNA-dependent RNA polymerase named 3Dpol. 5-Fluorouridine triphosphate (FUTP) is a potent competitive inhibitor of VPg uridylylation. Peptide analysis showed FUMP covalently linked to the Tyr3 of VPg. This fluorouridylylation prevents further incorporation of the second UMP residue. The molecular basis of how the incorporated FUMP blocks the incorporation of the second UMP is still unknown. To investigate the mechanism of inhibition of VPg uridylylation by FUMP, we have prepared a simplified 15-mer model of VPg1 containing FUMP and studied its x-ray crystal structure in complex with 3Dpol. Unfortunately, the fluorouridylylated VPg1 was disordered and not visible in the electron density maps; however, the structure of 3Dpol in the presence of VPg1-FUMP showed an 8 Å movement of the β9-α11 loop of the polymerase towards the active site cavity relative to the complex of 3Dpol with VPg1-UMP. The conformational rearrangement of this loop preceding the 3Dpol B motif seems to block the access of the template nucleotide to the catalytic cavity. This result may be useful in the design of new antivirals against not only FMDV but also other picornaviruses, since all members of this family require the uridylylation of their VPg proteins to initiate the viral RNA synthesis.

A Highly Divergent Antigenic Site of Foot-and-Mouth Disease Virus Retains Its Immunodominance

1995 ◽  
Vol 8 (1) ◽  
pp. 11-18 ◽  
Author(s):  
B. BORREGO ◽  
J.A. CAMARERO ◽  
M.G. MATEU ◽  
E. DOMINGO
Keyword(s):  
Disease Virus ◽  
Antigenic Site ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Fine mapping of a foot-and-mouth disease virus epitope recognized by serotype-independent monoclonal antibody 4B2

2011 ◽  
Vol 49 (1) ◽  
pp. 94-101 ◽  
Author(s):  
Yongzhong Yu ◽  
Haiwei Wang ◽  
Lei Zhao ◽  
Chunyuan Zhang ◽  
Zhigang Jiang ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Disease Virus ◽  
Fine Mapping ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Virus Epitope

A cyclic disulfide peptide reproduces in solution the main structural features of a native antigenic site of foot-and-mouth disease virus

1997 ◽  
Vol 20 (3) ◽  
pp. 209-219 ◽  
Author(s):  
Thomas Haack ◽  
Julio A. Camarero ◽  
Xavier Roig ◽  
Mauricio G. Mateu ◽  
Esteban Domingo ◽  
...  
Keyword(s):  
Disease Virus ◽  
Antigenic Site ◽  
Foot And Mouth Disease ◽  
Structural Features ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Identification of a conserved linear epitope on the VP1 protein of serotype O foot-and-mouth disease virus by neutralising monoclonal antibody 8E8

2011 ◽  
Vol 155 (1) ◽  
pp. 291-299 ◽  
Author(s):  
Decheng Yang ◽  
Chunyuan Zhang ◽  
Lei Zhao ◽  
Guohui Zhou ◽  
Haiwei Wang ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Linear Epitope ◽  
Vp1 Protein ◽  
Serotype O ◽  
Mouth Disease Virus ◽  
Foot And Mouth
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