Critical site differences of fusion protein between wildtype and vaccine measles virus strains in Indonesia

  • Made Setiawan Depattment of Child Health, Sulianti Saroso Infectious Disease Hospital, Jakarta
  • Agus Sjahrurachman Department of Microbiology, University of Indonesia Medical School, Jakarta
  • Fera Ibrahim Department of Microbiology, University of Indonesia Medical School, Jakarta
  • Agus Suwandono National Institute Health Research and Development
Keywords: tiiilJ type measles virus, measles vaccine, F protein, critical sites

Abstract

Background Measles virus can cause high morbidity and mortality in infants and children. Fusion glycoprotein (F protein) found in the viral envelope is important for the host cell infection mechanism. F protein is immunogenic and may cause specific immune responses in the host. High variability is found in the F protein gene of vaccine viral strains compared to 'Wild type strains. This amino add sequence variability may result in a less specific immune response against other strains, possibly rendering the
vaccine to be less effective.


Objective To detennine the amino add sequence differences in critical sites of F protein in Mld type and vaccine measles virus strains in Indonesia.


Methods We compared amino acid sequences of three genotypes of Mld type measles virus (02, 03 and D9) to those of the vaccine strains, CAM􀀸 70, Schwarz, and Edmonston􀀸wt type measles virus.


Resul ts Analysis showed that there were differences at Fl􀀸F2 cleavage site, B cell epitopes, and H protein binding site between the CAM􀀸70 vaccine viral strains and Mld type strains. Schwarz vaccine strain differed from the wild type strains at the H protein binding site. A 03 wild type strain potential glycosylation site was also different from all other strains studied.

Conclusion There were differences in the critical sites of F protein between Mld type strains and the CAM􀀸70 and Schwarz vaccine strains. 

References

1. World Health Organization. Global measles mortality reduction and regional elimination, 2000-2001. Part 1. Weekly Epidemiological Record. 2002;77A9·56.
2. Griffin DE, Bellini W]. Measles Virus. In: Fields Virology. 3rd ed. Philadelphia􀁡New York: Lippincott􀁡Raven; 1996. p. 1267·312.
3. Tyrell DIJ, Norrby F. Structural polypeptides of measles virus. J Gen Viro!. 1978;39,219·29.
4. Rima, BK. The proteins of morbilli viruses. J Gen Virol. 1983;64,1205·19.
5. Partidos CD, Salani FB, Ripley J, Steward MW Decon-structing the antigenic profile of a protective epitope from measles virus fusion protein using overlapping peptides. Vaccine. 2000;18,321-4.
6. Rota JS, Wang ZD, Rota PA, Bellini W]. Comparison of sequences of the H, F, and N coding genes of measles virus vaccine strains. Virus Res. 1994;31 :317-20.
7. Rota JS, Hummel KB, Rota PA , Bellini W].G enetic variability of the glycoprotein gene of current v.ild􀁡type measles isolates. Virology. 1992;188,135·42.
8. Komase K, Suzuki N, Nakayama T, Miki K, Kawanishi R, Fukuda K. Genome sequence of measles virus. NCBI no. accession, AB046218 (2001).A vailble from, http,//www.ncbi.nlm.nih.govlnuccorel.AB046218
9. Coligan JE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W Current protocols in immunology.V ol II.N ational Institute of Health of USA: Current Protocols Wiley; 1996. p.841.96.
10. Atabani SF, Obeid EO, Chargelegue D, Aaby p, Whittle H, Steward MW Identification of an immunodominant neutralizing and protective epitope from measles virus fusion protein by using human sera from acute infection. J Virol. 1997;7:7240·5.
11. Richardson C, Hull D, Greer P, Hasel K, Berkovich A, Englund G, et al. The nucleotide sequence of the mRNA encoding the fusion protein of measles virus (Edmonston Strain): A comparison of fusion protein from several different paramyxoviruses.V irology.1 986;1 55 :508-23.
12. Tsukiyama K, Yoshikawa Y, and Y amanouchi K. Fusion glycoprotein (F) of rinderpest virus: Entire nucleotide sequence of the F RNA, and several features of the F protein. Virology. 1988;164.523·30.
13. Fournier P, Bro\Vll NHC, Berbers GAM, Wiesmueller KH, Fleckenstein BT, Schneider F, et al.A ntibodies to a new linear site at the topographical or functional interface between the haemagglutinin and fusion proteins protect against measles encephalitis. J Gen Viro!. 1997;78,1295·302.
14. Alkhatib G, Shen SH, Briedis D, Richardson C, Roder J. Functional analysis of N􀁡linked glycosylation mutants of the measles virus fusion protein synthesized by recombinant vaccinia virus vectors.J Virol.1 994;68:1 522-31.
15. Hu A, Sheshberandaran H, Norbby E, and Kovamees ]. Molecular characterization of epitopes on the measles virus hemagglutinin protein.V irology.1 993;192:351A.
Published
2011-06-30
How to Cite
1.
Setiawan M, Sjahrurachman A, Ibrahim F, Suwandono A. Critical site differences of fusion protein between wildtype and vaccine measles virus strains in Indonesia. PI [Internet]. 30Jun.2011 [cited 29Jan.2023];51(3):123-. Available from: https://paediatricaindonesiana.org/index.php/paediatrica-indonesiana/article/view/508
Section
Articles
Received 2016-09-08
Accepted 2016-09-08
Published 2011-06-30