Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)

Sobrino, F.; Martinez, M. A.; Carrillo, C.; Beck, E.

Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)

The primary structure of VP3, VP2 and VP4 capsid protein genes has been determined for six epizootiologically-related foot-and-mouth disease virus (FMDV) isolates of serotype C1, two of which presented immunogenic differences as determined by a cross-protection assay. The results obtained have been compared with those previously reported for the corresponding VP1 genes Martinez et al.(1988) Gene 62, 75-84. High rates of fixation of mutations have been estimated for the four capsid protein genes that ranged from 3.9 × 10-4 to 4.5 × 10-3 substitutions per nucleotide per year, with the highest values corresponding to VP1. Despite this genetic heterogeneity most of the amino acid exchanges are within the VP1 protein. Of the fourteen amino acid substitutions one was located in VP2 and two in VP3. Five out of the eleven amino acid exchanges that affected VP1 were located within residues 138-149, part of a main immunogenic site in FMDV. These results show that in the course of a foot-and-mouth disease outbreak, immunologically relevant amino acid substitutions occur mainly in viral capsid protein VP1. © 1989.

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Main Authors:	Sobrino, F., Martinez, M. A., Carrillo, C., Beck, E.
Format:	journal article biblioteca
Language:	eng
Published:	1989
Online Access:	http://hdl.handle.net/20.500.12792/4356
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id	dig-inia-es-20.500.12792-4356
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spelling	dig-inia-es-20.500.12792-43562020-12-15T09:54:34Z Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1) Sobrino, F. Martinez, M. A. Carrillo, C. Beck, E. The primary structure of VP3, VP2 and VP4 capsid protein genes has been determined for six epizootiologically-related foot-and-mouth disease virus (FMDV) isolates of serotype C1, two of which presented immunogenic differences as determined by a cross-protection assay. The results obtained have been compared with those previously reported for the corresponding VP1 genes Martinez et al.(1988) Gene 62, 75-84. High rates of fixation of mutations have been estimated for the four capsid protein genes that ranged from 3.9 × 10-4 to 4.5 × 10-3 substitutions per nucleotide per year, with the highest values corresponding to VP1. Despite this genetic heterogeneity most of the amino acid exchanges are within the VP1 protein. Of the fourteen amino acid substitutions one was located in VP2 and two in VP3. Five out of the eleven amino acid exchanges that affected VP1 were located within residues 138-149, part of a main immunogenic site in FMDV. These results show that in the course of a foot-and-mouth disease outbreak, immunologically relevant amino acid substitutions occur mainly in viral capsid protein VP1. © 1989. 2020-10-22T16:51:46Z 2020-10-22T16:51:46Z 1989 journal article http://hdl.handle.net/20.500.12792/4356 10.1016/0168-1702(89)90021-X eng Attribution-NonCommercial-ShareAlike 4.0 International http://creativecommons.org/licenses/by-nc-sa/4.0/ open access
institution	INIA ES
collection	DSpace
country	España
countrycode	ES
component	Bibliográfico
access	En linea
databasecode	dig-inia-es
tag	biblioteca
region	Europa del Sur
libraryname	Biblioteca del INIA España
language	eng
description	The primary structure of VP3, VP2 and VP4 capsid protein genes has been determined for six epizootiologically-related foot-and-mouth disease virus (FMDV) isolates of serotype C1, two of which presented immunogenic differences as determined by a cross-protection assay. The results obtained have been compared with those previously reported for the corresponding VP1 genes Martinez et al.(1988) Gene 62, 75-84. High rates of fixation of mutations have been estimated for the four capsid protein genes that ranged from 3.9 × 10-4 to 4.5 × 10-3 substitutions per nucleotide per year, with the highest values corresponding to VP1. Despite this genetic heterogeneity most of the amino acid exchanges are within the VP1 protein. Of the fourteen amino acid substitutions one was located in VP2 and two in VP3. Five out of the eleven amino acid exchanges that affected VP1 were located within residues 138-149, part of a main immunogenic site in FMDV. These results show that in the course of a foot-and-mouth disease outbreak, immunologically relevant amino acid substitutions occur mainly in viral capsid protein VP1. © 1989.
format	journal article
author	Sobrino, F. Martinez, M. A. Carrillo, C. Beck, E.
spellingShingle	Sobrino, F. Martinez, M. A. Carrillo, C. Beck, E. Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
author_facet	Sobrino, F. Martinez, M. A. Carrillo, C. Beck, E.
author_sort	Sobrino, F.
title	Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
title_short	Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
title_full	Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
title_fullStr	Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
title_full_unstemmed	Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)
title_sort	antigenic variation of foot-and-mouth disease virus of serotype c during propagation in the field is mainly restricted to only one structural protein (vp1)
publishDate	1989
url	http://hdl.handle.net/20.500.12792/4356
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Antigenic variation of foot-and-mouth disease virus of serotype C during propagation in the field is mainly restricted to only one structural protein (VP1)

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