CHARACTERIZATION OF FSH AND LH ENCODING GENE SEQUENCES IN THE EGYPTIAN WATER BUFFALO (BUBALUS BUBALIS)

E.M. ABD EL FATTAH¹, S.F. DARWISH²*, A.M. EL BEHAIRY³, E.M. GOUDA⁴, S.Z. MOUSSA^5
1Biotechnology Research Unit, Animal Reproduction Research Institute, El-Haram, Giza, Egypt
²Biotechnology Research Unit, Animal Reproduction Research Institute, El-Haram, Giza, Egypt
³Biochemistry Department, Faculty of Veterinary Medicine, Cairo University, Egypt
⁴Biochemistry Department, Faculty of Veterinary Medicine, Cairo University, Egypt
⁵ Biochemistry Department, Faculty of Veterinary Medicine, Cairo University, Egypt
* Corresponding Author : samahtarek@hotmail.com

Received : 27-08-2015     Accepted : 27-10-2015     Published : 21-11-2015
Volume : 4     Issue : 2       Pages : 60 - 67
World Res J Agr Biotechnol 4.2 (2015):60-67

Keywords : Egyptian buffalo, FSH, LH, cDNAs, Molecular characterization
Academic Editor : Patel J. K., N. S. Kute
Conflict of Interest : None declared
Acknowledgements/Funding : We gratefully acknowledge Animal Reproduction Research Institute, Agricultural Research Center, Giza, Egypt for their financial support of this work.

Aiming to characterize the full length of cDNAs encoding FSHβ, LHβ and common α subunits of gonadotropins of the Egyptian Buffalo, total RNA of anterior pituitary was extracted and the gonadotropins subunits were amplified then, the coding cDNAs sequences of gonadotropin α common, FSHβ and LHβ subunits of Egyptian water buffalo (Bubalusbubalis) were determined. Both the nucleotide and deduced amino acid sequences were deposited in the GenBank as first record for Egyptian Buffalo and were compared with published Indian Buffalo sequences and that of other mammalian species. The open reading frames (ORF) for gonadotropin α common, FSHβ and LHβ subunits were 363, 390 and 426 bp long and encoded for 120, 129 and 141 amino acids, respectively. Alignment analysis showed great similarities to Indian buffalo, sheep, goat and cattle while they exhibit lower similarities to equines, rodents and primates. Generally, the main cysteine domains and putative glycosylation sites were conserved in all the subunits. Differences in the deduced amino acid sequence for FSHβ subunit were restricted to the third exon, especially Gly102 in Egyptian buffalo that replaced Ser102 in most reported Indian buffalo mature FSHβ protein sequences. In conclusion, the differences found between Egyptian and Indian water buffalo in Gonadotropin genes sequences can be attributed to polymorphism.