Characteristic in vitro evolution pattern of foot and mouth disease virus A81/Castellanos/Arg/87

The in vitro evolution of Foot and mouth disease virus (FMDV) A/81/Castellanos/Arg/87 (A/Castellanos/87) was studied by partial biological and biochemical characterization of viral populations selected after 25 passages on secondary fetal bovine kidney cell monolayers. These passages were performed...

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Bibliographic Details
Published in:Virus research 1997-05, Vol.48 (2), p.157-163
Main Authors: Mbayed, V, Schiappacassi, M, Corominas, A, Campos, R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Animals, Newborn
Antigenic Variation - immunology
Antigens, Viral - chemistry
Antigens, Viral - genetics
Antigens, Viral - immunology
Aphthovirus - genetics
Aphthovirus - immunology
Aphthovirus - pathogenicity
Attenuation
Base Sequence
Capsid - chemistry
Capsid - genetics
Capsid - immunology
Capsid Proteins
Cattle
Cell Line
Epitopes - chemistry
Epitopes - genetics
Evolution, Molecular
Foot and mouth disease virus
Genetic variants
Mice
Sequence Analysis, DNA
Viral evolution
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Summary:The in vitro evolution of Foot and mouth disease virus (FMDV) A/81/Castellanos/Arg/87 (A/Castellanos/87) was studied by partial biological and biochemical characterization of viral populations selected after 25 passages on secondary fetal bovine kidney cell monolayers. These passages were performed in the presence or absence of immune pressure exerted in the form of antiviral polyclonal serum. While the viral populations passaged in the absence of immune pressure acquired characteristics such as antigenic heterogeneity, VP1 amino acid modification and plaque size reduction, the populations selected after immune pressure also presented both neutralizing resistance and attenuation for suckling mice. The comparison with other previously studied FMDV strains suggests that FMDV A/Castellanos/87 adopts a differential response to immunological pressure and other selective forces. In addition, the sequencing analysis of viral selected populations shows a restriction in the number and type of amino acid replacements tolerated by FMDV capsid proteins.
ISSN:0168-1702
1872-7492
DOI:10.1016/S0168-1702(97)81605-X