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2.
Indian J Exp Biol ; 2013 Feb; 51(2): 124-128
Article in English | IMSEAR | ID: sea-147575

ABSTRACT

Out of 200 serum samples collected from cattle (142) and buffaloes (58) of various ages and sexand subjected to latex agglutination test (LAT) using serotype specific peptides (O, A, Asia 1) and also with peptide for non-structural protein 2B (NSP-2B), 114 (70%) samples were positive against FMDV type ‘O’, 102 (51%) against serotype ‘A’ and 104 (52%) against serotype ‘Asia 1’. With NSP-2B peptide a total of 71 (35.5%) samples were positive. The results suggest that LAT could be used for the diagnosis of foot and mouth disease virus as it is easy, cheap and effective test.


Subject(s)
Amino Acid Sequence , Animals , Cattle , Foot-and-Mouth Disease/immunology , Foot-and-Mouth Disease Virus/classification , Latex Fixation Tests/methods , Microspheres , Molecular Sequence Data , Peptides/chemistry , Peptides/immunology , Serotyping , Vaccination , Viral Nonstructural Proteins/immunology
3.
Journal of Veterinary Science ; : 65-73, 2011.
Article in English | WPRIM | ID: wpr-47187

ABSTRACT

This study describes the expression of heat shock protein70 (HSP70) and alpha-basic-crystallin (alpha-BC) and their association with apoptosis and some related adaptor proteins in the pathogenesis of foot-and-mouth disease virus (FMDV)-induced myocarditis in lambs. HSP70 was generally overexpressed in the myocardial tissues and inflammatory cells of FMDV-induced myocarditis with differential accumulation and localization in same hearts when compared to non-foot-and-mouth disease control hearts. alpha-BC immunolabeling showed coarse aggregations in the Z line of the cardiomyocytes in FMDV-infected hearts in contrast to control hearts. Overall, the results of this study show that the anti-apoptotic proteins, HSP70 and alpha-BC, were overexpressed with increased apoptosis in FMDV-infected heart tissues. Both proteins failed to protect the cardiomyocytes from apoptosis as defense mechanisms to the FMDV during the infection, suggesting that the virus is able to increase apoptosis via both downregulation and/or upregulation of these anti-apoptotic proteins.


Subject(s)
Animals , Apoptosis Regulatory Proteins/metabolism , Foot-and-Mouth Disease/complications , Foot-and-Mouth Disease Virus/classification , Gene Expression , HSP70 Heat-Shock Proteins/metabolism , Myocarditis/complications , Myocardium/pathology , Sheep , Sheep Diseases/virology , Turkey , alpha-Crystallin B Chain/metabolism
4.
Journal of Veterinary Science ; : 363-371, 2011.
Article in English | WPRIM | ID: wpr-17400

ABSTRACT

The nucleotide sequence of the VP1 (1D) and partial 3D polymerase (3Dpol) coding regions of the foot and mouth disease virus (FMDV) vaccine strain A/Iran87, a highly passaged isolate (~150 passages), was determined and aligned with previously published FMDV serotype A sequences. Overall analysis of the amino acid substitutions revealed that the partial 3Dpol coding region contained four amino acid alterations. Amino acid sequence comparison of the VP1 coding region of the field isolates revealed deletions in the highly passaged Iranian isolate (A/Iran87). The prominent G-H loop of the FMDV VP1 protein contains the conserved arginine-glycine-aspartic acid (RGD) tripeptide, which is a well-known ligand for a specific cell surface integrin. Despite losing the RGD sequence of the VP1 protein and an Asp26-->Glu substitution in a beta sheet located within a small groove of the 3Dpol protein, the virus grew in BHK 21 suspension cell cultures. Since this strain has been used as a vaccine strain, it may be inferred that the RGD deletion has no critical role in virus attachment to the cell during the initiation of infection. It is probable that this FMDV subtype can utilize other pathways for cell attachment.


Subject(s)
Amino Acid Sequence , Amino Acid Substitution , Antigens, Viral/chemistry , Capsid Proteins/chemistry , Cloning, Molecular , Foot-and-Mouth Disease Virus/classification , Gene Expression Regulation, Viral , Molecular Sequence Data , Phylogeny , Viral Nonstructural Proteins/chemistry
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