Spectroscopic characterization of two peptides derived from the stem of rabies virus glycoprotein.
Rabies virus glycoprotein (G) is a trimeric type I transmembrane glycoprotein that mediates both receptor recognition and low pH-induced membrane fusion. Electron microscopy has indicated that the ectodomain of protein G is made of a globular head and a stem. In order to characterize the putative stem region at the molecular level, we designed two peptides, P(S) and P(L), which were produced as GST fusion proteins in bacteria. Peptide P(S) extends from amino acid (aa) 374 to aa 428 whereas peptide P(L) extends from aa 368 down to the end of the ectodomain of G (aa 439). Their secondary and quaternary structures have been studied with spectroscopic and biophysical methods. We show that these isolated peptides are monomeric and poorly structured in aqueous solution. However, circular dichroism (CD) in presence of 2,2,2-trifluoroethanol and NMR data indicate that this region may adopt a alpha-helical conformation in the complete glycoprotein.
Maillard
Antoine
A
Laboratoire de Virologie Moléculaire et Structurale, CNRS, 91198 Gif sur Yvette Cedex, France.
Domanski
Michaël
M
Brunet
Patrick
P
Chaffotte
Alain
A
Guittet
Eric
E
Gaudin
Yves
Y
D000595:Amino Acid Sequence; D000956:Antigens, Viral; D002942:Circular Dichroism; D006023:Glycoproteins / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014759:Viral Envelope Proteins / Q000737:chemistry*
D000956:Antigens, Viral; D006023:Glycoproteins; D010455:Peptides; D014759:Viral Envelope Proteins; C064951:glycoprotein G, Rabies virus