NDLI: Characterization of Membrane-bound and Membrane Anchor-less Forms of Hemagglutinin Glycoprotein of Rinderpest Virus Expressed by Baculovirus Recombinants

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Characterization of Membrane-bound and Membrane Anchor-less Forms of Hemagglutinin Glycoprotein of Rinderpest Virus Expressed by Baculovirus Recombinants

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Virus Genes : Volume 14, Issue 1, January 1997

Characterization of Membrane-bound and Membrane Anchor-less Forms of Hemagglutinin Glycoprotein of Rinderpest Virus Expressed by Baculovirus Recombinants

Content Provider	Springer Nature Link
Author	Naik, Sangeeta Shaila, MS
Copyright Year	1997
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.
Starting Page	95
Ending Page	104
Page Count	10
File Format	PDF
ISSN	09208569
Journal	Virus Genes
Volume Number	14
Issue Number	2
e-ISSN	1572994X
Language	English
Publisher	Kluwer Academic Publishers
Publisher Date	1997-01-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Medical Microbiology Virology Plant Sciences
Content Type	Text
Resource Type	Article
Subject	Virology Genetics Medicine Molecular Biology

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