Literature DB >> 10403702

Capsid protein-encoding (P1) sequence of foot and mouth disease virus type Asia 1 ind 63/72.

G R Reddy1, J D Tratschin, C Natarajan, V V Suryanarayana.   

Abstract

Variations in the amino acid sequence of Foot-and-Mouth Disease Virus (FMDV) structural proteins are the basis for the antigenic diversity of the virus. Majority of antigenic sites for the virus neutralization are present on VP1, the major immunogenic protein. However, a few conformational epitopes are present on the structural proteins VP2 and VP3. The nucleotide sequence encoding all the four structural proteins (P1 region) of FMDV type Asia 1 Ind 63/72 was determined. The nucleotide and the deduced amino acid sequence of P1 of Asia 1 of Indian strain was compared with that of Asia 1 Israel strain. Differences were observed at 284 (14%) nucleotide positions resulting in 69 (10%) amino acid changes. The variation in the derived amino acid sequence is the highest in VP1 (14.4%) followed by VP2 (10%), VP3 (6.4%) and VP4 (3%). Deletion of two amino acids, which was observed in the case of Indian strain as well as in Israel strain indicated that these deletions are specific for type Asia 1. The P1 sequence was also compared with the corresponding region of the other serotypes O1K, A12, Cl and SAT-1. The sequence has been submitted to EMBL data bank, under accession number Y09949.

Entities:  

Mesh:

Substances:

Year:  1999        PMID: 10403702     DOI: 10.1023/a:1008076805196

Source DB:  PubMed          Journal:  Virus Genes        ISSN: 0920-8569            Impact factor:   2.332


  13 in total

1.  Neutralization of foot-and-mouth disease virus can be mediated through any of at least three separate antigenic sites.

Authors:  Q C Xie; D McCahon; J R Crowther; G J Belsham; K C McCullough
Journal:  J Gen Virol       Date:  1987-06       Impact factor: 3.891

2.  The three-dimensional structure of foot-and-mouth disease virus at 2.9 A resolution.

Authors:  R Acharya; E Fry; D Stuart; G Fox; D Rowlands; F Brown
Journal:  Nature       Date:  1989-02-23       Impact factor: 49.962

3.  Antigenic sites on foot-and-mouth disease virus type A10.

Authors:  A A Thomas; R J Woortmeijer; W Puijk; S J Barteling
Journal:  J Virol       Date:  1988-08       Impact factor: 5.103

4.  Antigenic variation in Foot and Mouth Disease Virus type Asia 1 isolates circulated during 1993-95 in India.

Authors:  P Tulasiram; M Tyagi; K Srinivas; K Prabhudas; C Natarajan; V Suryanarayana
Journal:  Virus Genes       Date:  1997       Impact factor: 2.332

5.  Nucleotide and amino acid sequence coding for polypeptides of foot-and-mouth disease virus type A12.

Authors:  B H Robertson; M J Grubman; G N Weddell; D M Moore; J D Welsh; T Fischer; D J Dowbenko; D G Yansura; B Small; D G Kleid
Journal:  J Virol       Date:  1985-06       Impact factor: 5.103

6.  Sequence analysis of monoclonal antibody resistant mutants of type O foot and mouth disease virus: evidence for the involvement of the three surface exposed capsid proteins in four antigenic sites.

Authors:  J D Kitson; D McCahon; G J Belsham
Journal:  Virology       Date:  1990-11       Impact factor: 3.616

7.  The nucleotide sequence of the structural-protein-coding region of foot-and-mouth disease virus serotype SAT3.

Authors:  A L Brown; R O Campbell; B E Clarke
Journal:  Gene       Date:  1989-02-20       Impact factor: 3.688

8.  The capsid protein-encoding sequence of foot-and-mouth disease virus O2Brescia.

Authors:  O Krebs; H G Berger; O Marquardt
Journal:  Arch Virol       Date:  1991       Impact factor: 2.574

9.  Nucleotide sequence of the P1 region of serotype Asia1 foot-and-mouth disease virus.

Authors:  Y Stram; O Laor; T Molad; D Chai; D Moore; H Yadin; Y Becker
Journal:  Virus Genes       Date:  1994-07       Impact factor: 2.332

10.  Structure of the FMDV translation initiation site and of the structural proteins.

Authors:  E Beck; S Forss; K Strebel; R Cattaneo; G Feil
Journal:  Nucleic Acids Res       Date:  1983-11-25       Impact factor: 16.971

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.