Effects of Different Continium Dielectric Models in a Molecular Dynamics and Energy Minimization Study of the Antigenic Loop of Foot-and-Mouth Disease Virus

1993 ◽  
Vol 11 (2) ◽  
pp. 429-441 ◽  
Author(s):  
M. Cristina Vega ◽  
Carlos Alemán ◽  
Cristóbal Alhambra ◽  
Juan J. Perez
Keyword(s):  
Molecular Dynamics ◽  
Disease Virus ◽  
Energy Minimization ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Molecular dynamics of the α-helical epitope of a novel synthetic lipopeptide foot-and-mouth disease virus vaccine

Biopolymers ◽  
1989 ◽  
Vol 28 (1) ◽  
pp. 499-512 ◽  
Author(s):  
Michael Krug ◽  
Gerd Folkers ◽  
Bernd Haas ◽  
Günter Hess ◽  
Karl-Heinz Wiesmüller ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Disease Virus ◽  
Virus Vaccine ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Residue L143 of the Foot-and-Mouth Disease Virus Leader Proteinase Is a Determinant of Cleavage Specificity

2008 ◽  
Vol 82 (9) ◽  
pp. 4656-4659 ◽  
Author(s):  
Christina Mayer ◽  
David Neubauer ◽  
Aloysius T. Nchinda ◽  
Regina Cencic ◽  
Katja Trompf ◽  
...  
Keyword(s):  
Disease Virus ◽  
Energy Minimization ◽  
Cleavage Site ◽  
Foot And Mouth Disease ◽  
Peptide Bond ◽  
Mouth Disease ◽  
Cleavage Specificity ◽  
Fmdv Serotypes ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT The foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) self-processes inefficiently at the Lpro/VP4 cleavage site LysLeuLys*GlyAlaGly (* indicates cleaved peptide bond) when the leucine at position P2 is replaced by phenylalanine. Molecular modeling and energy minimization identified the Lpro residue L143 as being responsible for this discrimination. The variant Lpro L143A self-processed efficiently at the Lpro/VP4 cleavage site containing P2 phenylalanine, whereas the L143M variant did not. Lpro L143A self-processing at the eIF4GII sequence AspPheGly*ArgGlnThr was improved but showed more-extensive aberrant processing. Residue 143 in Lpro is occupied only by leucine and methionine in all sequenced FMDV serotypes, implying that these bulky side chains are one determinant of the restricted specificity of Lpro.

High resolution surface structure of foot-and-mouth disease virus

1978 ◽  
Vol 36 (2) ◽  
pp. 376-377
Author(s):  
S. S. Breese ◽  
H. L. Bachrach
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Surface Structure ◽  
Disease Virus ◽  
Potassium Phosphate ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Physical Measurements ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Models for the structure of foot-and-mouth disease virus (FMDV) have been proposed from chemical and physical measurements (Brown, et al., 1970; Talbot and Brown, 1972; Strohmaier and Adam, 1976) and from rotational image-enhancement electron microscopy (Breese, et al., 1965). In this report we examine the surface structure of FMDV particles by high resolution electron microscopy and compare it with that of particles in which the outermost capsid protein VP3 (ca. 30, 000 daltons) has been split into smaller segments, two of which VP3a and VP3b have molecular weights of about 15, 000 daltons (Bachrach, et al., 1975).Highly purified and concentrated type A12, strain 119 FMDV (5 mg/ml) was prepared as previously described (Bachrach, et al., 1964) and stored at 4°C in 0. 2 M KC1-0. 5 M potassium phosphate buffer at pH 7. 5. For electron microscopy, 1. 0 ml samples of purified virus and trypsin-treated virus were dialyzed at 4°C against 0. 2 M NH4OAC at pH 7. 3, deposited onto carbonized formvar-coated copper screens and stained with phosphotungstic acid, pH 7. 3.

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