Characterization of membrane-bound and membrane anchor-less forms of hemagglutinin glycoprotein of Rinderpest virus expressed by baculovirus recombinants

Naik, S and Shaila, MS (1997) Characterization of membrane-bound and membrane anchor-less forms of hemagglutinin glycoprotein of Rinderpest virus expressed by baculovirus recombinants. In: Virus Genes, 14 (2). pp. 95-104.

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Abstract

The Rinderpest virus (RPV) hemagglutinin (H) is a class 2 glycoprotein by means of which the virus attaches to the host cell receptor, A full length cDNA coding for H protein was used to construct a recombinant baculovirus expressing the H protein, recH(M), on the surface of insect cells. The small N terminal cytoplasmic domain was deleted and the transmembrane domain which extends from amino acids 35 to 59 was replaced with a signal peptide derived from the ecdysteroid UDP glycosyl transferase (egt) gene of the baculovirus, AcNPV. The protein recH(sec) expressed by the recombinant baculovirus carrying this engineered gene was secreted into the medium. Both forms of recombinant H protein retained reactivity with conformation-dependent monoclonal antibodies, The recH(M) was recognized by antibodies made in cattle either as the result of vaccination or natural infection. The soluble form of H is a valuable tool for studying the structure and function of the RPV H glycoprotein.

Item Type:	Journal Article
Publication:	Virus Genes
Publisher:	Springer
Additional Information:	Copyright of this article belongs to Springer.
Keywords:	Rinderpest virus;hemagglutinin;recombinant baculovirus;secretory hemagglutinin.
Department/Centre:	Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited:	29 May 2009 06:56
Last Modified:	19 Sep 2010 05:24
URI:	http://eprints.iisc.ac.in/id/eprint/18681

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