Prokaryotic expression and molecular characterization of surface antigen 3 (SAG 3) protein of Toxoplasma gondii


155 / 75

Authors

  • VIKRANT SUDAN Indian Veterinary Research Institute, Izatnagar, Uttar Pradesh 243 122 India
  • ANUP KUMAR TEWARI Indian Veterinary Research Institute, Izatnagar, Uttar Pradesh 243 122 India
  • HARKIRAT SINGH GADVASU, Ludhiana
  • B C SARAVANAN Indian Veterinary Research Institute, Izatnagar, Uttar Pradesh 243 122 India

https://doi.org/10.56093/ijans.v84i8.43209

Keywords:

Expression, Molecular characterization, RH Strain, SAG3, Toxoplasma gondii

Abstract

Toxoplasmosis, caused by Toxoplasma gondii, is an important zoonotic disease with worldwide prevalence. In the present communication, we report molecular cloning, heterologous expression and characterization of 1158 bp complete open reading frame (ORF) of surface antigen 3 (SAG3) of T. gondii, RH strain, IVRI stock for the first time from India. The rSAG3 protein was expressed in E. coli as a 46kDa histidine-tagged fusion protein. Sequence analysis of the SAG3 coding sequence revealed 99.9% homology with the published sequence of T. gondii RH strain with substitution of a single base adenosine ‘A’ with guanosine ‘G’ at nucleotide position 397 in the ORF. Substitution of a single nucleotide resulted in substitution of aspartic acid (D) residue replacing asparagine (N).

Downloads

Download data is not yet available.

References

Ajzenberg D, Ban˜ulsb A L, Suc C, Dume‘trea A, Demard M, Carmed B and Darde´a M L. 2004. Genetic diversity, clonality and sexuality in Toxoplasma gondii. International Journal of Parasitology 34: 1185. DOI: https://doi.org/10.1016/j.ijpara.2004.06.007

Burg J L, Perelman D, Kasper L H, Ware P L and Boothroyd J C.1988. Molecular analysis for gene encoding the major surface antigens of Toxoplasma gondii. Journal of Immunology 141: 3584. DOI: https://doi.org/10.4049/jimmunol.141.10.3584

Cesbron-Delauw M F, Tomavo S, Beauchamps P, Fourmaux M P,Camus D, Capron A and Dubermetz J F. 1994. Similarities between the primary structures of two distinct major surface protein of Toxoplasma gondii. Journal of Biological Chemistry 269: 16217. DOI: https://doi.org/10.1016/S0021-9258(17)33995-9

D³ugoñska H. 2008. Toxoplasma gondii—known and unknown parasite. Wiadomosci Parazytologiczne 54: 199–204.

Dubey J P. 2004.Toxoplasmosis- a waterborne zoonosis. Veterinary Parasitology 126: 57. DOI: https://doi.org/10.1016/j.vetpar.2004.09.005

Dubey J P. 1993. Toxoplasma, Neospora, Sarcocystis, and other tissue cyst forming coccidia of humans and animals. Kreier JP, editor.2nd ed. Parasitic Protozoa 6: 1– 158. DOI: https://doi.org/10.1016/B978-0-12-426016-0.50006-7

Ferguson D J. 2002. Toxoplasma gondii and sex: essential or optional extra? Trends in Parasitology 18: 355. DOI: https://doi.org/10.1016/S1471-4922(02)02330-9

Fux B, Rodrigues C V, Portela R W, Silva N M, Su C, Sibley D, Vitor R W A and Gazzinelli R T. 2003. Role of cytokines and major histocompatibility complex restriction in mouse resistance to infection with a natural recombinant strain (Type I-III) of Toxoplasma gondii. Infecion and Immunity 71: 6392. DOI: https://doi.org/10.1128/IAI.71.11.6392-6401.2003

Gautam O P, Chhabra M B, Bhardwaj R M, Gupta S L and Kalita C C.1979. Current status of toxoplasmosis research in India. The First All India Seminar on Toxoplasmosis. Department of Veterinary Medicine, HAU.

Grigg M E, Bonnefoy S, Hehl A B, Suzuki Y and Boothroyd J C. 2001. Success and virulence in Toxoplasma as the result of sexual recombination between two distinct ancestries. Science 294: 161. DOI: https://doi.org/10.1126/science.1061888

Gross U, Müller W A, Knapp S. and Heesemann J. 1991. Identification of a virulence-associated antigen of Toxoplasma gondii by a mouse monoclonal antibody. Infection and Immunity 59: 4511. DOI: https://doi.org/10.1128/iai.59.12.4511-4516.1991

Hill D and Dubey J P. 2002. Toxoplasma gondii: Transmission, diagnosis and prevention. Clinical Microbiology and Infection 8: 634. DOI: https://doi.org/10.1046/j.1469-0691.2002.00485.x

Howe D K and Sibley L D. 1995. Toxoplasma gondii comprises three clonal lineages: correlation of parasite genotype with human disease. Journal of Infectious Diseases 172: 1561. DOI: https://doi.org/10.1093/infdis/172.6.1561

Jacquet A, Coulon L, Neve J D, Daminet V, Haumont M, Garcia L, Bollin A, Jurado M and Biemans R. 2001. The surface antigen SAG3 mediates the attachment of Toxoplasma gondii to cell-surface proteoglycans. Molecular and Biochemical Parasitology 116: 35. DOI: https://doi.org/10.1016/S0166-6851(01)00297-3

Kazemi B, Maghen L, Bandehpour M, Shahabi S and Haghighi. A. 2007. Gene cloning of P43 surface protein of Toxoplasma gondii tachyzoite and bradyzoite (SAG3). Gene Therapy and Molecular Biology 11: 113.

Montoya J G and Liesenfeld O.2004. Toxoplasmosis. Lancet 363: 1965. DOI: https://doi.org/10.1016/S0140-6736(04)16412-X

Sambrook J, Fritch E F and Maniatis T. 1989. Molecular Cloning: A Laboratory Manual. 2nd edn. Cold spring harbor Laboratory press.

Su C, Evans D, Cole R H, Kissinger J C, Ajioka J W and Sibley L D. 2003. Recent expansion of Toxoplasma through enhanced oral transmission. Science 299: 414. DOI: https://doi.org/10.1126/science.1078035

Velmurugan G V, Tewari A K, Rao J R, Baidya S, Udaya K M and Mishra A K. 2008. High level expression of SAG1 and GRA7 gene of Toxoplasma gondii (Izatnagar isolate) and their application in serodiagnosis of goat toxoplasmosis. Veterinary Parasitology 154: 185–92. DOI: https://doi.org/10.1016/j.vetpar.2008.03.032

Downloads

Submitted

2014-08-12

Published

2014-08-14

Issue

Section

Articles

How to Cite

SUDAN, V., TEWARI, A. K., SINGH, H., & SARAVANAN, B. C. (2014). Prokaryotic expression and molecular characterization of surface antigen 3 (SAG 3) protein of Toxoplasma gondii. The Indian Journal of Animal Sciences, 84(8), 824–828. https://doi.org/10.56093/ijans.v84i8.43209
Citation